|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2282 |
3.58e-158 |
|
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: 493.31 E-value: 3.58e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1933 RFVGLTNLGATCYLASTIQQLYMIPEARQAVFT---AKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPfcKTYTMDK 2009
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTD--KTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2010 QPLNTGEQKDMTEFFTDLITKVEEMSP--ELKNTVKSLFGGVITNNVVSLDCEHVSqtAEEFYTVRCQVADM--KNIYES 2085
Cdd:cd02659 79 DSLNTFEQHDVQEFFRVLFDKLEEKLKgtGQEGLIKNLFGGKLVNYIICKECPHES--EREEYFLDLQVAVKgkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2086 LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLM 2165
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2166 GksdrkegfKDVGDHSKDTESYEYDLIGVTVHTGTADGGHYYSFIRDIVnphaykNNKWYLFNDAEVKPFDSAQLASECF 2245
Cdd:cd02659 237 K--------KEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPNDAEEECF 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 403420571 2246 GGEMTTKTYDSVtdkfmDFSFEKTHSAYMLFYKRMEP 2282
Cdd:cd02659 303 GGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1935-2277 |
3.00e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 213.84 E-value: 3.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1935 VGLTNLGATCYLASTIQQLYMIPEARQAVF----TAKYSEDMKHKTTLLELQKMFTYL-MESECKAYNPRPFCKTYTMDK 2009
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLrispLSEDSRYNKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2010 QPLNTGEQKDMTEFFTDLITKVEE-MSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKN--- 2081
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEdLNGnhstENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2082 ---IYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPLRLDMTP 2158
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2159 YTEDflmgksdrkegfkdvGDHSKDTESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPfdsa 2238
Cdd:pfam00443 239 YLAE---------------ELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK------AYENNRWYKFDDEKVTE---- 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 403420571 2239 qlasecfggemttktydsVTDKFMdfsfEKTHSAYMLFY 2277
Cdd:pfam00443 294 ------------------VDEETA----VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1936-2278 |
1.02e-55 |
|
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: 195.78 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplntg 2015
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2016 EQKDMTEFFTDLITKVEEM----------SPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KN 2081
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEElkksskrtsdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKglpqVS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2082 IYESLDEVTIKDTLEGDNMYTCSHCgKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDMTPYTE 2161
Cdd:cd02257 101 LEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2162 DFLMgksdrkegfkdvgDHSKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphayKNNKWYLFNDAEVKPfdsaql 2240
Cdd:cd02257 179 EGEK-------------DSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDP------SDGKWYKFNDDKVTE------ 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 403420571 2241 asecfggemttktydsVTDKFMDFSFEKTHSAYMLFYK 2278
Cdd:cd02257 234 ----------------VSEEEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2278 |
7.39e-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: 195.72 E-value: 7.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHK-----------TTLLELQKMFTYLMESECKAYNPRPFCKT 2004
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKnmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2005 YTmdkqpLNTGEQKDMTEFFTDLITKVE-----EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM 2079
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEaklskSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2080 KNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPY 2159
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2160 TEDflmgksdrkegfkdvgdhsKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSA 2238
Cdd:cd02668 236 LAE-------------------SDEGSYVYELSGVLIHQGVsAYSGHYIAHIKD------EQTGEWYKFNDEDVEEMPGK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 403420571 2239 QLasECFGGEMTTKTYDSVTDKfmdfSFEKTHSAYMLFYK 2278
Cdd:cd02668 291 PL--KLGNSEDPAKPRKSEIKK----GTHSSRTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2277 |
2.46e-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: 153.20 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKT--TLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLN 2013
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2014 TGEQKDMTEFFTDLITKVE-----------EMSPELKNT--VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK 2080
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMQkacldrfkklkAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2081 NIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMmkEKVNTHFSFPLRLDMTPYt 2160
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RG--GKINKQISFPETLDLSPY- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2161 edflMgkSDRKEGfkdvgdhskdteSYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphaykNNKWYLFNDAEVKPFDSAQ 2239
Cdd:cd02661 238 ----M--SQPNDG------------PLKYKLYAVLVHSGFsPHSGHYYCYVKSS-------NGKWYNMDDSKVSPVSIET 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 403420571 2240 LASEcfggemttktydsvtdkfmdfsfekthSAYMLFY 2277
Cdd:cd02661 293 VLSQ---------------------------KAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1920-2285 |
3.87e-37 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 154.64 E-value: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1920 WDYWPHEDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFtYLMESECKAYNPR 1999
Cdd:COG5077 179 WHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLF-YNLQTGEEPVDTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2000 PFCKTYTMDKqpLNTGEQKDMTEFFTDLITKVEE--MSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA 2077
Cdd:COG5077 258 ELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKsmRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2078 DMKNIYESLDEVTIKDTLEGDNMYTCSHCGkKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMT 2157
Cdd:COG5077 336 GMKNLQESFRRYIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2158 PytedFLMGKSDRKEgfkdvgdhSKDtesYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPFDS 2237
Cdd:COG5077 415 P----FLDRDADKSE--------NSD---AVYVLYGVLVHSGDLHEGHYYALLK------PEKDGRWYKFDDTRVTRATE 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 403420571 2238 AQLASECFGGEMTTKtydsvtDKFMDFS-FEKTHSAYMLFYKRMEPEEE 2285
Cdd:COG5077 474 KEVLEENFGGDHPYK------DKIRDHSgIKRFMSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2245 |
7.01e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 137.89 E-value: 7.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLL----ELQKMFTYLMESEckayNPRPFCKTYTM---- 2007
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSclscAMDEIFQEFYYSG----DRSPYGPINLLylsw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2008 -DKQPLNTGEQKDMTEFFTDLITKVEEMS---PELKNTVKS-------LFGGVITNNVVSLDCEHVSQTAEEF------- 2069
Cdd:cd02660 78 kHSRNLAGYSQQDAHEFFQFLLDQLHTHYggdKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFldlsldi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2070 --------YTVRCQVADMKNIYESLDEVTIKDTLeGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMK 2141
Cdd:cd02660 158 pnkstpswALGESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL-NKTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2142 EKVNTHFSFPLRLDMTPYTedflmgksdrKEGFKDVGDHSKDTESYEYDLIGVTVHTGTADGGHYYSFIRdivnphaYKN 2221
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYT----------SSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCR-------QGD 298
|
330 340
....*....|....*....|....*
gi 403420571 2222 NKWYLFNDAEVKPFDSAQ-LASECF 2245
Cdd:cd02660 299 GQWFKFDDAMITRVSEEEvLKSQAY 323
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2278 |
9.96e-31 |
|
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: 122.78 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLymipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplnTG 2015
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------------------------------------------------SA 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2016 EQKDMTEFFTDLITkveemspELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK------NIYESLDEV 2089
Cdd:cd02674 21 DQQDAQEFLLFLLD-------GLHSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLF 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2090 TIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPLR-LDMTPYTedflmgks 2168
Cdd:cd02674 94 TKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR--FSFSRGSTRKLTTPVTFPLNdLDLTPYV-------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2169 drkegfkdvgDHSKDTESYEYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPfdsaqlasecfgge 2248
Cdd:cd02674 164 ----------DTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKN------NETNDWYKFDDSRVTK-------------- 213
|
330 340 350
....*....|....*....|....*....|
gi 403420571 2249 mttktydsvtdkfMDFSFEKTHSAYMLFYK 2278
Cdd:cd02674 214 -------------VSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2278 |
6.84e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 117.59 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNP--------RPfcktytm 2007
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpdyfleasRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2008 dkQPLNTGEQKDMTEFFTDLITKveemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVR---CQVADMKNIYE 2084
Cdd:cd02664 74 --PWFTPGSQQDCSEYLRYLLDR-------LHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDlsfPSVQDLLNYFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2085 SldevtiKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFL 2164
Cdd:cd02664 145 S------PEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2165 MGKSDRKEGFKDVGDHSKDTESYEYDLIGVTVHTGTA-DGGHYYSFIRDIVN----------PHAYKNNK----WYLFND 2229
Cdd:cd02664 219 SESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpePKDAEENDesknWYLFND 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 403420571 2230 AEVkpfdsaqlaSECfggemTTKTYDSVTdkfmdfSFEKTHSAYMLFYK 2278
Cdd:cd02664 299 SRV---------TFS-----SFESVQNVT------SRFPKDTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2212 |
6.45e-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 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: 104.78 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPeARQAVFtakySEDMKhkttllelqKMFtylmeSECKAYNPRpfcktytmdkqpLNTG 2015
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP-ALRELL----SETPK---------ELF-----SQVCRKAPQ------------FKGY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2016 EQKDMTEFFTDLITKveemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KNIYESLDEVTI 2091
Cdd:cd02667 50 QQQDSHELLRYLLDG-------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEikseCSIESCLKQFTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2092 KDTLEGDNMYTCSHCgkkVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKeKVNTHFSFPLRLDMTPytedFLMGKSDrk 2171
Cdd:cd02667 123 VEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAP----FCDPKCN-- 192
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 403420571 2172 egfkdvgdHSKDTESYEYDLIGVTVHTGTADGGHYYSFIRD 2212
Cdd:cd02667 193 --------SSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2278 |
1.55e-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 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: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPEARQAV--FTAKYSEDMKHKTTLL-ELQKMFTyLMESECKAYNPRPFCKTYTM----- 2007
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQSSDNLTnALRDLFD-TMDKKQEPVPPIEFLQLLRMafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2008 -DKQPLNTGEQKDMTEFFTDLITKVE---EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQ-TAEEFYTVRCQVaDMKNI 2082
Cdd:cd02657 80 aEKQNQGGYAQQDAEECWSQLLSVLSqklPGAGSKGSFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHI-SITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2083 YESLDEvTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTpyteD 2162
Cdd:cd02657 159 VNYLQD-GLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY----E 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2163 FLmgksdrkegfkdvgdhskdTESYEYDLIGVTVHTG-TADGGHYYSFIRDivnphaYKNNKWYLFNDA---EVKPFDSA 2238
Cdd:cd02657 234 LC-------------------TPSGYYELVAVITHQGrSADSGHYVAWVRR------KNDGKWIKFDDDkvsEVTEEDIL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 403420571 2239 QLASecfGGEmttktydsvtdkfmdfsfekTHSAYMLFYK 2278
Cdd:cd02657 289 KLSG---GGD--------------------WHIAYILLYK 305
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2278 |
2.05e-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: 103.54 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYmipearqavftakysedmkHKTTLLELQKMFTYLMESECK--AYNPRPFCKTYTMDKQPLN 2013
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRtgVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2014 TGEQKDMTEFFTDLITKV------------------EEMSPELKNT-VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRC 2074
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIaeildaerkaekanrklnNNNNAEPQPTwVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2075 QVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRL 2154
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2155 DMTPYTEDflMGKSDRkegfkdvgdhskdtesyEYDLIGVTVHTG-TADGGHYYSFIRdivnphayKNNKWYLFNDAEVK 2233
Cdd:cd02663 222 RLFNTTDD--AENPDR-----------------LYELVAVVVHIGgGPNHGHYVSIVK--------SHGGWLLFDDETVE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 403420571 2234 PFDSAQLAsECFGGEMTTKTydsvtdkfmdfsfekthsAYMLFYK 2278
Cdd:cd02663 275 KIDENAVE-EFFGDSPNQAT------------------AYVLFYQ 300
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2232 |
2.82e-21 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 97.78 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPEARQAVFT--AKYSEDMKHKTTLLELQ--KMFT------YLMESECKAYN-------- 1997
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVDPANDLNCQliKLADgllsgrYSKPASLKSENdpyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1998 PRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKVE-EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQV 2076
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDrESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2077 ADMKNIYESLDE-----VTIKDTLEG-----DNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvtmmKEKVnt 2146
Cdd:cd02658 161 PKDEATEKEEGElvyepVPLEDCLKAyfapeTIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL-----ENWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2147 hfsfPLRLDMTPYTEDFLMGKsdrkegfkdvgdhskdtesyEYDLIGVTVHTGT-ADGGHYYSFIRDIVNPhaykNNKWY 2225
Cdd:cd02658 234 ----PKKLDVPIDVPEELGPG--------------------KYELIAFISHKGTsVHSGHYVAHIKKEIDG----EGKWV 285
|
....*..
gi 403420571 2226 LFNDAEV 2232
Cdd:cd02658 286 LFNDEKV 292
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1934-2233 |
1.34e-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: 84.17 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1934 FVGLTNLGATCYLASTIQQLYMIPearqavftaKYSEDMKHKTTLL----ELQKMFTYLME---SECKAYNPRPFCKTyT 2006
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLIssveQLQSSFLLNPEkynDELANQAPRRLLNA-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2007 MDKQPLNTG-EQKDMTEFFTDLITKVEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA-DMKNIYE 2084
Cdd:cd02671 94 REVNPMYEGyLQHDAQEVLQCILGNIQEL-------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQeSELSKSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2085 SLDEVTIKDTLE------------------GDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMK----E 2142
Cdd:cd02671 167 ESSEISPDPKTEmktlkwaisqfasverivGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCygglS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2143 KVNTHFSFPLRLDmtpytedfLMGKSDRKegfkdvgdhskdtESYEYDLIGVTVHTG-TADGGHYYSFIRdivnphaykn 2221
Cdd:cd02671 247 KVNTPLLTPLKLS--------LEEWSTKP-------------KNDVYRLFAVVMHSGaTISSGHYTAYVR---------- 295
|
330
....*....|..
gi 403420571 2222 nkWYLFNDAEVK 2233
Cdd:cd02671 296 --WLLFDDSEVK 305
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1935-2229 |
4.46e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 81.93 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1935 VGLTNLGATCYLASTIQQLYMIPEARQ-AVFTAKySEDMKHKTTLLELQKMFTYLMESE---CKAYNprpFCKTytMDKQ 2010
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLA-TECLKEHCLLCELGFLFDMLEKAKgknCQASN---FLRA--LSSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2011 P-------LNTGEQKDMTEFFTDLITK-----VEEMSPELK----------NTVKSLFGGVITNNVVSLDCEHVSQTAEE 2068
Cdd:pfam13423 75 PeasalglLDEDRETNSAISLSSLIQSfnrflLDQLSSEENstppnpspaeSPLEQLFGIDAETTIRCSNCGHESVRESS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2069 FYTVRCQVADMKNIYESLDEVT-----IKDTLEGDNMY--TCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVtmmK 2141
Cdd:pfam13423 155 THVLDLIYPRKPSSNNKKPPNQtfssiLKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWR---Q 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2142 EKVNTHFsFPLRLDMTPYTedflmgksdrkegfkdvgDHSKDTESYEYDLIGVTVHTGTADG-GHYYSFIR-DIVNPHAY 2219
Cdd:pfam13423 232 LWKTPGW-LPPEIGLTLSD------------------DLQGDNEIVKYELRGVVVHIGDSGTsGHLVSFVKvADSELEDP 292
|
330
....*....|
gi 403420571 2220 KNNKWYLFND 2229
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1936-2279 |
1.18e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 80.23 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQL---------YMIPEARQA-VFTAKYSEDMKHKTtLLELQKMFTYLMESECKAYNPRPfckty 2005
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldeLLDDLSKELkVLKNVIRKPEPDLN-QEEALKLFTALWSSKEHKVGWIP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2006 tmdkqplNTGEQKDMTEFFTDLItkvEEMSPELKNTVKSLFGGVITNNVVSLDCE----HVS----QTAEEFYTVRCQVA 2077
Cdd:COG5533 75 -------PMGSQEDAHELLGKLL---DELKLDLVNSFTIRIFKTTKDKKKTSTGDwfdiIIElpdqTWVNNLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2078 DMKniYESLDEVTIKdtlEGDNMytcshcGKKVRA--EKRACFKKLPRILSFNTMRYTF-NMVTMMKEKVNTHFSFPLRL 2154
Cdd:COG5533 145 NME--ELVDDETGVK---AKENE------ELEVQAkqEYEVSFVKLPKILTIQLKRFANlGGNQKIDTEVDEKFELPVKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2155 DMTpytedflmgKSDRKEGFkdvgdhskdtesyeYDLIGVTVHTGTADGGHYYSFIRdivnphayKNNKWYLFNDAEVKP 2234
Cdd:COG5533 214 DQI---------LNIVKETY--------------YDLVGFVLHQGSLEGGHYIAYVK--------KGGKWEKANDSDVTP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 403420571 2235 FDSaqlasecfggemtTKTYDsvtdkfmdfsfEKTHSAYMLFYKR 2279
Cdd:COG5533 263 VSE-------------EEAIN-----------EKAKNAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2247 |
5.64e-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: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYmipearqavftaKYSEDMKHKTTLLelqkmFTYLMES-ECKAYNPRPfcktytmDKQPLNt 2014
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF------------SQQQDVSEFTHLL-----LDWLEDAfQAAAEAISP-------GEKSKN- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2015 geqkDMTEFFTdlitkveemspELKNTVKSLFGGVITNNvvsldcehvsqtaEEFYTVRCQVADMKNIYESLDEVTIKDT 2094
Cdd:cd02665 56 ----PMVQLFY-----------GTFLTEGVLEGKPFCNC-------------ETFGQYPLQVNGYGNLHECLEAAMFEGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2095 LEGDnmytcsHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPlrldmtpytedflmgksdrkegf 2174
Cdd:cd02665 108 VELL------PSDHSVKSGQERWFTELPPVLTFELSRFEFN--QGRPEKIHDKLEFP----------------------- 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 403420571 2175 kdvgdhsKDTESYEYDLIGVTVHTGTADGGHYYSFIRDivNPHayknNKWYLFNDAEVKPFDSAQLASECFGG 2247
Cdd:cd02665 157 -------QIIQQVPYELHAVLVHEGQANAGHYWAYIYK--QSR----QEWEKYNDISVTESSWEEVERDSFGG 216
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1934-2233 |
6.30e-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: 67.73 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1934 FVGLTNLGATCYLASTIQQLYMIPEARQavFTAKYSEDMKHKTTLLELQKMFTYLMEsecKAYNPRPFcKTY-------- 2005
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRN--FFLLYENYENIKDRKSELVKRLSELIR---KIWNPRNF-KGHvsphellq 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2006 ---TMDKQPLNTGEQKDMTEFFTDLITKV----EEMSPELKNTVKSLFGGVITN-----NVVSLDCEHVSQTAEEFYTVr 2073
Cdd:cd02669 193 avsKVSKKKFSITEQSDPVEFLSWLLNTLhkdlGGSKKPNSSIIHDCFQGKVQIetqkiKPHAEEEGSKDKFFKDSRVK- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2074 cQVADMKNIYESLD-----------------EVTIKDTLEGDNMYTCSHCGKKVraeKRACFKKLPRILSFNTMRYTFNm 2136
Cdd:cd02669 272 -KTSVSPFLLLTLDlpppplfkdgneeniipQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSKN- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2137 vTMMKEKVNTHFSFPLR-LDMTPYTEDFLmgksdrkegfKDVGDHSKdtesyeYDLIGVTVHTGT-ADGGHYYSFIRDiv 2214
Cdd:cd02669 347 -NFFKEKNPTIVNFPIKnLDLSDYVHFDK----------PSLNLSTK------YNLVANIVHEGTpQEDGTWRVQLRH-- 407
|
330
....*....|....*....
gi 403420571 2215 nphaYKNNKWYLFNDAEVK 2233
Cdd:cd02669 408 ----KSTNKWFEIQDLNVK 422
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
2047-2279 |
5.09e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.67 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2047 GGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYES--------LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACF 2118
Cdd:COG5560 634 GQMNFNDAVVISCEWEEKRYLSLFSYDPLWTIREIGAAErtitlqdcLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2119 KKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPL-RLDMTPYTedflmgksdrkegfkdvgdHSKDTESYEYDLIGVTVH 2197
Cdd:COG5560 714 WRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIdDLDLSGVE-------------------YMVDDPRLIYDLYAVDNH 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2198 TGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSAqlasecfggemttktyDSVTDkfmdfsfekthSAYMLFY 2277
Cdd:COG5560 773 YGGLSGGHYTAYARN------FANNGWYLFDDSRITEVDPE----------------DSVTS-----------SAYVLFY 819
|
..
gi 403420571 2278 KR 2279
Cdd:COG5560 820 RR 821
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2400-2733 |
1.60e-08 |
|
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: 60.01 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2400 QILIKCPNQIVRQMFQRLCIHVIQRLrpvHAHLYLQPGMEDGSDDMDAsvEDIGGRSCVTRFVRTLLLIMEHgVKPHSKH 2479
Cdd:pfam12030 6 ELLLRNPDAEVRSAFGKLIVFALHKL---KELYGLPDGPCDPDDLEEE--WRSLSDSVLEAVVALLDHLWKE-FHTHLRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2480 LTEYFAFLYEFAKMGEEESQFLLS---LQAISTMVHFYMGTKGPENPQ-VEVLSEEegeeeeeeedilslaeEKYRPAAL 2555
Cdd:pfam12030 80 WDEYFGLLLSYANLGPREVAQLLDlgfLLKCLEIIAADEGDGPPLKYQyARMLRLV----------------EKRRPPSY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2556 EKMIALVALLVEQSRSERHLTLSQT---DMAALTGGKGFPF------LFQH-------------IRDGINIRQTCNLIFS 2613
Cdd:pfam12030 144 EKLIQLLSVLLRCCDLSLPPQSINEgaePLPNSLPDGPFPLtseeadLLRPlgrtngsifvkklLEIDQNPEATRKILRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2614 LCRYNNRLAEHIVSMLFTSIAK-LTPEAANPFFKLLTMLMEFAGGPPgtppfasyilqRIWEVIEYNPSQC--------- 2683
Cdd:pfam12030 224 LLWENPELSDSILKTLLWGIRGaPAHLLRDPFLRAAIVFCEDSWQAH-----------RIHNLIDHVAKQAdslnntegr 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2684 --LDWL--AVQTPRNKL------AHSWVLQNMENWVErFLLAHNYPRVRTSAAYLLVSLI 2733
Cdd:pfam12030 293 afLHFFkrAYQCINCRLgfdkewFASQVLENIPDWAP-PLLSYPDSNVRSETEDFLQEEL 351
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1936-2277 |
1.40e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 55.45 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1936 GLTNLGATCYLASTIQQLYMIPearqavftakysedmkhkttllelqkmftYLMEseckaynprpFCKTYTmdkqplntg 2015
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP-----------------------------SLIE----------YLEEFL--------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2016 EQKDMTEFFTDLITKVEemspelkNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEvtiKDTL 2095
Cdd:cd02662 33 EQQDAHELFQVLLETLE-------QLLKFPFDGLLASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTL---EHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2096 EGDNM------YTCSHCgkkvraekRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDmtpytedflmgksd 2169
Cdd:cd02662 103 DDFLSteiiddYKCDRC--------QTVIVRLPQILCIHLSRSVFDG-RGTSTKNSCKVSFPERLP-------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2170 rkegfkdvgdhskdteSYEYDLIGVTVHTGTADGGHYYSFIR-----------DIVNPHAYKN---NKWYLFNDAEVKpf 2235
Cdd:cd02662 160 ----------------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepgSFVRMREGPSstsHPWWRISDTTVK-- 221
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 403420571 2236 dsaqlasECfggemttKTYDSVTDKfmdfsfekthSAYMLFY 2277
Cdd:cd02662 222 -------EV-------SESEVLEQK----------SAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1935-2232 |
1.21e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 50.57 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1935 VGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYS----EDMKHKTTLL------------------ELQKMFTYLMESE 1992
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaelASDYPTERRIggrevsrselqrsnqfvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 1993 CKAYNPRPFCKTYTMDKQplNTGEQKDMTEFFTDLITK---VEEMSPELKNT------VKSLFGG--------VITNNVV 2055
Cdd:cd02666 82 TRSVTPSKELAYLALRQQ--DVTECIDNVLFQLEVALEpisNAFAGPDTEDDkeqsdlIKRLFSGktkqqlvpESMGNQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2056 SLDC--EHVSQTA----EEFYTVRCQvADMKNIYESLDEVtikdtLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNT 2129
Cdd:cd02666 160 SVRTktERFLSLLvdvgKKGREIVVL-LEPKDLYDALDRY-----FDYDSLTKLPQRSQVQAQLAQPLQRELISMDRYEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2130 MRYTFNMVTMMKEKVNTHFSfplRLDMTPYTEDFLmgKSDRKEGFKDVgdhskdtESYEYDLIGVTVHTGTADGGHYYSF 2209
Cdd:cd02666 234 PSSIDDIDELIREAIQSESS---LVRQAQNELAEL--KHEIEKQFDDL-------KSYGYRLHAVFIHRGEASSGHYWVY 301
|
330 340
....*....|....*....|...
gi 403420571 2210 IRDivnphaYKNNKWYLFNDAEV 2232
Cdd:cd02666 302 IKD------FEENVWRKYNDETV 318
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2016-2278 |
6.54e-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: 47.52 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2016 EQKDMTEFFTDLITKVEEMSPELKntvkslfggvitnnvvsLDCEHVSQTAEEfytvrcqvaDMKNIYESLDEVTIKDTl 2095
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEPK-----------------VDIIHGGKKDQD---------DDKLVNERLLQIPVPDD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2096 EGDNMYTCSHCGKkvRAEKRACFKKLPRILSFNTMRYTfnMVTMMKEKVNTHFSFPLRLDMTPYTED----FLMGKSDRK 2171
Cdd:cd02670 75 DDGGGITLEQCLE--QYFNNSVFAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDIPDFVADdpraCSKCQLECR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403420571 2172 EGFKDVgDHSKDTESYEYDLIGVTVHTGTA-DGGHYYSFIR-----DIVNPHAYKNNKWYLFndaevkpfDSAQLASECF 2245
Cdd:cd02670 151 VCYDDK-DFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVRygsysLTETDNEAYNAQWVFF--------DDMADRDGVS 221
|
250 260 270
....*....|....*....|....*....|...
gi 403420571 2246 GGemttktyDSVTDKFmdfsfeKTHSAYMLFYK 2278
Cdd:cd02670 222 NG-------FNIPAAR------LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2184-2236 |
1.94e-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: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 403420571 2184 TESYEYDLIGVTVHTGTAD-GGHYYSFIRDIvnPHAYKNNKWYLFNDAEVKPFD 2236
Cdd:cd02672 208 ESIYKYELVGYVCEINDSSrGQHNVVFVIKV--NEESTHGRWYLFNDFLVTPVS 259
|
|
| |
