|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1930-2279 |
3.65e-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: 492.93 E-value: 3.65e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1930 RFVGLTNLGATCYLASTIQQLYMIPEARQAVFT---AKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPfcKTYTMDK 2006
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTD--KTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2007 QPLNTGEQKDMTEFFTDLITKVEEMSP--ELKNTVKSLFGGVITNNVVSLDCEHVSqtAEEFYTVRCQVADM--KNIYES 2082
Cdd:cd02659 79 DSLNTFEQHDVQEFFRVLFDKLEEKLKgtGQEGLIKNLFGGKLVNYIICKECPHES--EREEYFLDLQVAVKgkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2083 LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLM 2162
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2163 GksdrkegfKDVGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRDIVnphaykNNKWYLFNDAEVKPFDSAQLASECF 2242
Cdd:cd02659 237 K--------KEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPNDAEEECF 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 568969975 2243 GGEMTTKTYDSVtdkfmDFSFEKTHSAYMLFYKRMEP 2279
Cdd:cd02659 303 GGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1932-2274 |
1.73e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 214.61 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1932 VGLTNLGATCYLASTIQQLYMIPEARQAVF----TAKYSEDMKHKTTLLELQKMFTYL-MESECKAYNPRPFCKTYTMDK 2006
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLrispLSEDSRYNKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2007 QPLNTGEQKDMTEFFTDLITKVEE-MSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKN--- 2078
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEdLNGnhstENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2079 ---IYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPLRLDMTP 2155
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2156 YTEDflmgksdrkegfkdvGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPfdsa 2235
Cdd:pfam00443 239 YLAE---------------ELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK------AYENNRWYKFDDEKVTE---- 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 568969975 2236 qlasecfggemttktydsVTDKFMdfsfEKTHSAYMLFY 2274
Cdd:pfam00443 294 ------------------VDEETA----VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1933-2275 |
1.22e-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: 195.39 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplntg 2012
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2013 EQKDMTEFFTDLITKVEEM----------SPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KN 2078
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEElkksskrtsdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKglpqVS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2079 IYESLDEVTIKDTLEGDNMYTCSHCgKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDMTPYTE 2158
Cdd:cd02257 101 LEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2159 DFLMgksdrkegfkdvgDRSKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphayKNNKWYLFNDAEVKPfdsaql 2237
Cdd:cd02257 179 EGEK-------------DSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDP------SDGKWYKFNDDKVTE------ 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 568969975 2238 asecfggemttktydsVTDKFMDFSFEKTHSAYMLFYK 2275
Cdd:cd02257 234 ----------------VSEEEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2275 |
9.49e-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: 195.33 E-value: 9.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHK-----------TTLLELQKMFTYLMESECKAYNPRPFCKT 2001
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKnmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2002 YTmdkqpLNTGEQKDMTEFFTDLITKVE-----EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM 2076
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEaklskSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2077 KNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPY 2156
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2157 TEDflmgksdrkegfkdvgdrsKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSA 2235
Cdd:cd02668 236 LAE-------------------SDEGSYVYELSGVLIHQGVsAYSGHYIAHIKD------EQTGEWYKFNDEDVEEMPGK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568969975 2236 QLasECFGGEMTTKTYDSVTDKfmdfSFEKTHSAYMLFYK 2275
Cdd:cd02668 291 PL--KLGNSEDPAKPRKSEIKK----GTHSSRTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2274 |
2.34e-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: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKT--TLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLN 2010
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2011 TGEQKDMTEFFTDLITKVE-----------EMSPELKNT--VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK 2077
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMQkacldrfkklkAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2078 NIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMmkEKVNTHFSFPLRLDMTPYt 2157
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RG--GKINKQISFPETLDLSPY- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2158 edflMgkSDRKEGfkdvgdrskdteSYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphaykNNKWYLFNDAEVKPFDSAQ 2236
Cdd:cd02661 238 ----M--SQPNDG------------PLKYKLYAVLVHSGFsPHSGHYYCYVKSS-------NGKWYNMDDSKVSPVSIET 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 568969975 2237 LASEcfggemttktydsvtdkfmdfsfekthSAYMLFY 2274
Cdd:cd02661 293 VLSQ---------------------------KAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1917-2282 |
3.90e-37 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 154.64 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1917 WDYWPHEDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFtYLMESECKAYNPR 1996
Cdd:COG5077 179 WHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLF-YNLQTGEEPVDTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1997 PFCKTYTMDKqpLNTGEQKDMTEFFTDLITKVEE--MSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA 2074
Cdd:COG5077 258 ELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKsmRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2075 DMKNIYESLDEVTIKDTLEGDNMYTCSHCGkKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMT 2154
Cdd:COG5077 336 GMKNLQESFRRYIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2155 PytedFLMGKSDRKEgfkdvgdrSKDtesYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPFDS 2234
Cdd:COG5077 415 P----FLDRDADKSE--------NSD---AVYVLYGVLVHSGDLHEGHYYALLK------PEKDGRWYKFDDTRVTRATE 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568969975 2235 AQLASECFGGEMTTKtydsvtDKFMDFS-FEKTHSAYMLFYKRMEPEEE 2282
Cdd:COG5077 474 KEVLEENFGGDHPYK------DKIRDHSgIKRFMSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2242 |
4.79e-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: 138.66 E-value: 4.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLL----ELQKMFTYLMESEckayNPRPFCKTYTM---- 2004
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSclscAMDEIFQEFYYSG----DRSPYGPINLLylsw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2005 -DKQPLNTGEQKDMTEFFTDLITKVEEMS---PELKNTVKS-------LFGGVITNNVVSLDCEHVSQTAEEF------- 2066
Cdd:cd02660 78 kHSRNLAGYSQQDAHEFFQFLLDQLHTHYggdKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFldlsldi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2067 --------YTVRCQVADMKNIYESLDEVTIKDTLeGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMK 2138
Cdd:cd02660 158 pnkstpswALGESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL-NKTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2139 EKVNTHFSFPLRLDMTPYTedflmgksdrKEGFKDVGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRdivnphaYKN 2218
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYT----------SSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCR-------QGD 298
|
330 340
....*....|....*....|....*
gi 568969975 2219 NKWYLFNDAEVKPFDSAQ-LASECF 2242
Cdd:cd02660 299 GQWFKFDDAMITRVSEEEvLKSQAY 323
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2275 |
1.76e-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: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLymipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplnTG 2012
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------------------------------------------------SA 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2013 EQKDMTEFFTDLITkveemspELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK------NIYESLDEV 2086
Cdd:cd02674 21 DQQDAQEFLLFLLD-------GLHSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLF 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2087 TIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPLR-LDMTPYTEDflmgkS 2165
Cdd:cd02674 94 TKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR--FSFSRGSTRKLTTPVTFPLNdLDLTPYVDT-----R 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2166 DRKEGFKdvgdrskdtesyeYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPfdsaqlasecfgge 2245
Cdd:cd02674 167 SFTGPFK-------------YDLYAVVNHYGSLNGGHYTAYCKN------NETNDWYKFDDSRVTK-------------- 213
|
330 340 350
....*....|....*....|....*....|
gi 568969975 2246 mttktydsvtdkfMDFSFEKTHSAYMLFYK 2275
Cdd:cd02674 214 -------------VSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2275 |
6.22e-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: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNP--------RPfcktytm 2004
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpdyfleasRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2005 dkQPLNTGEQKDMTEFFTDLITKveemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVR---CQVADMKNIYE 2081
Cdd:cd02664 74 --PWFTPGSQQDCSEYLRYLLDR-------LHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDlsfPSVQDLLNYFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2082 SldevtiKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFL 2161
Cdd:cd02664 145 S------PEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2162 MGKSDRKEGFKDVGDRSKDTESYEYDLIGVTVHTGTA-DGGHYYSFIRDIVN----------PHAYKNNK----WYLFND 2226
Cdd:cd02664 219 SESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpePKDAEENDesknWYLFND 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568969975 2227 AEVkpfdsaqlaSECfggemTTKTYDSVTdkfmdfSFEKTHSAYMLFYK 2275
Cdd:cd02664 299 SRV---------TFS-----SFESVQNVT------SRFPKDTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2209 |
1.02e-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: 104.01 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPeARQAVFtakySEDMKhkttllelqKMFtylmeSECKAYNPRpfcktytmdkqpLNTG 2012
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP-ALRELL----SETPK---------ELF-----SQVCRKAPQ------------FKGY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2013 EQKDMTEFFTDLITKveemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KNIYESLDEVTI 2088
Cdd:cd02667 50 QQQDSHELLRYLLDG-------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEikseCSIESCLKQFTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2089 KDTLEGDNMYTCSHCgkkVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKeKVNTHFSFPLRLDMTPytedFLMGKSDRK 2168
Cdd:cd02667 123 VEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAP----FCDPKCNSS 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568969975 2169 EgfkdvgdrskDTESYEYDLIGVTVHTGTADGGHYYSFIRD 2209
Cdd:cd02667 195 E----------DKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2275 |
1.43e-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: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPEARQAV--FTAKYSEDMKHKTTLL-ELQKMFTyLMESECKAYNPRPFCKTYTM----- 2004
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQSSDNLTnALRDLFD-TMDKKQEPVPPIEFLQLLRMafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2005 -DKQPLNTGEQKDMTEFFTDLITKVE---EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQ-TAEEFYTVRCQVaDMKNI 2079
Cdd:cd02657 80 aEKQNQGGYAQQDAEECWSQLLSVLSqklPGAGSKGSFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHI-SITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2080 YESLDEvTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTpyteD 2159
Cdd:cd02657 159 VNYLQD-GLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY----E 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2160 FLmgksdrkegfkdvgdrskdTESYEYDLIGVTVHTG-TADGGHYYSFIRDivnphaYKNNKWYLFNDA---EVKPFDSA 2235
Cdd:cd02657 234 LC-------------------TPSGYYELVAVITHQGrSADSGHYVAWVRR------KNDGKWIKFDDDkvsEVTEEDIL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568969975 2236 QLASecfGGEmttktydsvtdkfmdfsfekTHSAYMLFYK 2275
Cdd:cd02657 289 KLSG---GGD--------------------WHIAYILLYK 305
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2275 |
2.17e-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: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYmipearqavftakysedmkHKTTLLELQKMFTYLMESECK--AYNPRPFCKTYTMDKQPLN 2010
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRtgVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2011 TGEQKDMTEFFTDLITKV------------------EEMSPELKNT-VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRC 2071
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIaeildaerkaekanrklnNNNNAEPQPTwVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2072 QVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRL 2151
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2152 DMTPYTEDflMGKSDRkegfkdvgdrskdtesyEYDLIGVTVHTG-TADGGHYYSFIRdivnphayKNNKWYLFNDAEVK 2230
Cdd:cd02663 222 RLFNTTDD--AENPDR-----------------LYELVAVVVHIGgGPNHGHYVSIVK--------SHGGWLLFDDETVE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568969975 2231 PFDSAQLAsECFGGEMTTKTydsvtdkfmdfsfekthsAYMLFYK 2275
Cdd:cd02663 275 KIDENAVE-EFFGDSPNQAT------------------AYVLFYQ 300
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2229 |
3.01e-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: 97.39 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPEARQAVFT--AKYSEDMKHKTTLLELQ--KMFT------YLMESECKAYN-------- 1994
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVDPANDLNCQliKLADgllsgrYSKPASLKSENdpyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1995 PRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKVE-EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQV 2073
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDrESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2074 ADMKNIYESLDE-----VTIKDTLEG-----DNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvtmmKEKVnt 2143
Cdd:cd02658 161 PKDEATEKEEGElvyepVPLEDCLKAyfapeTIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL-----ENWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2144 hfsfPLRLDMTPYTEDFLMGKsdrkegfkdvgdrskdtesyEYDLIGVTVHTGT-ADGGHYYSFIRDIVNPhaykNNKWY 2222
Cdd:cd02658 234 ----PKKLDVPIDVPEELGPG--------------------KYELIAFISHKGTsVHSGHYVAHIKKEIDG----EGKWV 285
|
....*..
gi 568969975 2223 LFNDAEV 2229
Cdd:cd02658 286 LFNDEKV 292
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1931-2230 |
1.30e-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: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1931 FVGLTNLGATCYLASTIQQLYMIPearqavftaKYSEDMKHKTTLL----ELQKMFTYLME---SECKAYNPRPFCKTyT 2003
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLIssveQLQSSFLLNPEkynDELANQAPRRLLNA-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2004 MDKQPLNTG-EQKDMTEFFTDLITKVEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA-DMKNIYE 2081
Cdd:cd02671 94 REVNPMYEGyLQHDAQEVLQCILGNIQEL-------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQeSELSKSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2082 SLDEVTIKDTLE------------------GDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMK----E 2139
Cdd:cd02671 167 ESSEISPDPKTEmktlkwaisqfasverivGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCygglS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2140 KVNTHFSFPLRLDmtpytedfLMGKSDRKegfkdvgdrskdtESYEYDLIGVTVHTG-TADGGHYYSFIRdivnphaykn 2218
Cdd:cd02671 247 KVNTPLLTPLKLS--------LEEWSTKP-------------KNDVYRLFAVVMHSGaTISSGHYTAYVR---------- 295
|
330
....*....|..
gi 568969975 2219 nkWYLFNDAEVK 2230
Cdd:cd02671 296 --WLLFDDSEVK 305
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1932-2226 |
5.62e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 81.93 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1932 VGLTNLGATCYLASTIQQLYMIPEARQ-AVFTAKySEDMKHKTTLLELQKMFTYLMESE---CKAYNprpFCKTytMDKQ 2007
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLA-TECLKEHCLLCELGFLFDMLEKAKgknCQASN---FLRA--LSSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2008 P-------LNTGEQKDMTEFFTDLITK-----VEEMSPELK----------NTVKSLFGGVITNNVVSLDCEHVSQTAEE 2065
Cdd:pfam13423 75 PeasalglLDEDRETNSAISLSSLIQSfnrflLDQLSSEENstppnpspaeSPLEQLFGIDAETTIRCSNCGHESVRESS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2066 FYTVRCQVADMKNIYESLDEVT-----IKDTLEGDNMY--TCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVtmmK 2138
Cdd:pfam13423 155 THVLDLIYPRKPSSNNKKPPNQtfssiLKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWR---Q 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2139 EKVNTHFsFPLRLDMTPYTedflmgksdrkegfkdvgDRSKDTESYEYDLIGVTVHTGTADG-GHYYSFIR-DIVNPHAY 2216
Cdd:pfam13423 232 LWKTPGW-LPPEIGLTLSD------------------DLQGDNEIVKYELRGVVVHIGDSGTsGHLVSFVKvADSELEDP 292
|
330
....*....|
gi 568969975 2217 KNNKWYLFND 2226
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1933-2276 |
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 568969975 1933 GLTNLGATCYLASTIQQL---------YMIPEARQA-VFTAKYSEDMKHKTtLLELQKMFTYLMESECKAYNPRPfckty 2002
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldeLLDDLSKELkVLKNVIRKPEPDLN-QEEALKLFTALWSSKEHKVGWIP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2003 tmdkqplNTGEQKDMTEFFTDLItkvEEMSPELKNTVKSLFGGVITNNVVSLDCE----HVS----QTAEEFYTVRCQVA 2074
Cdd:COG5533 75 -------PMGSQEDAHELLGKLL---DELKLDLVNSFTIRIFKTTKDKKKTSTGDwfdiIIElpdqTWVNNLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2075 DMKniYESLDEVTIKdtlEGDNMytcshcGKKVRA--EKRACFKKLPRILSFNTMRYTF-NMVTMMKEKVNTHFSFPLRL 2151
Cdd:COG5533 145 NME--ELVDDETGVK---AKENE------ELEVQAkqEYEVSFVKLPKILTIQLKRFANlGGNQKIDTEVDEKFELPVKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2152 DMTpytedflmgKSDRKEGFkdvgdrskdtesyeYDLIGVTVHTGTADGGHYYSFIRdivnphayKNNKWYLFNDAEVKP 2231
Cdd:COG5533 214 DQI---------LNIVKETY--------------YDLVGFVLHQGSLEGGHYIAYVK--------KGGKWEKANDSDVTP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568969975 2232 FDSaqlasecfggemtTKTYDsvtdkfmdfsfEKTHSAYMLFYKR 2276
Cdd:COG5533 263 VSE-------------EEAIN-----------EKAKNAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2244 |
5.04e-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: 65.66 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYmipearqavftaKYSEDMKHKTTLLelqkmFTYLMES-ECKAYNPRPfcktytmDKQPLNt 2011
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF------------SQQQDVSEFTHLL-----LDWLEDAfQAAAEAISP-------GEKSKN- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2012 geqkDMTEFFTdlitkveemspELKNTVKSLFGGVITNNvvsldcehvsqtaEEFYTVRCQVADMKNIYESLDEVTIKDT 2091
Cdd:cd02665 56 ----PMVQLFY-----------GTFLTEGVLEGKPFCNC-------------ETFGQYPLQVNGYGNLHECLEAAMFEGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2092 LEGDnmytcsHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPlrldmtpytedflmgksdrkegf 2171
Cdd:cd02665 108 VELL------PSDHSVKSGQERWFTELPPVLTFELSRFEFN--QGRPEKIHDKLEFP----------------------- 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568969975 2172 kdvgdrsKDTESYEYDLIGVTVHTGTADGGHYYSFIRDivNPHayknNKWYLFNDAEVKPFDSAQLASECFGG 2244
Cdd:cd02665 157 -------QIIQQVPYELHAVLVHEGQANAGHYWAYIYK--QSR----QEWEKYNDISVTESSWEEVERDSFGG 216
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1931-2230 |
8.33e-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: 67.34 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1931 FVGLTNLGATCYLASTIQQLYMIPEARQavFTAKYSEDMKHKTTLLELQKMFTYLMEsecKAYNPRPFcKTY-------- 2002
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRN--FFLLYENYENIKDRKSELVKRLSELIR---KIWNPRNF-KGHvsphellq 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2003 ---TMDKQPLNTGEQKDMTEFFTDLITKV----EEMSPELKNTVKSLFGGVITN-----NVVSLDCEHVSQTAEEFYTVr 2070
Cdd:cd02669 193 avsKVSKKKFSITEQSDPVEFLSWLLNTLhkdlGGSKKPNSSIIHDCFQGKVQIetqkiKPHAEEEGSKDKFFKDSRVK- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2071 cQVADMKNIYESLD-----------------EVTIKDTLEGDNMYTCSHCGKKVraeKRACFKKLPRILSFNTMRYTFNm 2133
Cdd:cd02669 272 -KTSVSPFLLLTLDlpppplfkdgneeniipQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSKN- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2134 vTMMKEKVNTHFSFPLR-LDMTPYTEDflmgksdrkegfkdvgDRSKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDiv 2211
Cdd:cd02669 347 -NFFKEKNPTIVNFPIKnLDLSDYVHF----------------DKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRH-- 407
|
330
....*....|....*....
gi 568969975 2212 nphaYKNNKWYLFNDAEVK 2230
Cdd:cd02669 408 ----KSTNKWFEIQDLNVK 422
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
2044-2276 |
7.39e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.29 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2044 GGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYES--------LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACF 2115
Cdd:COG5560 634 GQMNFNDAVVISCEWEEKRYLSLFSYDPLWTIREIGAAErtitlqdcLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2116 KKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPL-RLDMTPYTEdflmgksdrkegfkdvgdrSKDTESYEYDLIGVTVH 2194
Cdd:COG5560 714 WRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIdDLDLSGVEY-------------------MVDDPRLIYDLYAVDNH 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2195 TGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSAqlasecfggemttktyDSVTDkfmdfsfekthSAYMLFY 2274
Cdd:COG5560 773 YGGLSGGHYTAYARN------FANNGWYLFDDSRITEVDPE----------------DSVTS-----------SAYVLFY 819
|
..
gi 568969975 2275 KR 2276
Cdd:COG5560 820 RR 821
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2397-2730 |
1.52e-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: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2397 QILIKCPNQIVRQMFQRLCIHVIQRLrpvHAHLYLQPGMEDGSDDMDAsvEDIGGRSCVTRFVRTLLLIMEHgVKPHSKH 2476
Cdd:pfam12030 6 ELLLRNPDAEVRSAFGKLIVFALHKL---KELYGLPDGPCDPDDLEEE--WRSLSDSVLEAVVALLDHLWKE-FHTHLRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2477 LTEYFAFLYEFAKMGEEESQFLLS---LQAISTMVHFYMGTKGPENPQ-VEVLSEEegeeeeeeedilslaeEKYRPAAL 2552
Cdd:pfam12030 80 WDEYFGLLLSYANLGPREVAQLLDlgfLLKCLEIIAADEGDGPPLKYQyARMLRLV----------------EKRRPPSY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2553 EKMIALVALLVEQSRSERHLTLSQT---DMAALTGGKGFPF------LFQH-------------IRDGINIRQTCNLIFS 2610
Cdd:pfam12030 144 EKLIQLLSVLLRCCDLSLPPQSINEgaePLPNSLPDGPFPLtseeadLLRPlgrtngsifvkklLEIDQNPEATRKILRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2611 LCRYNNRLAEHIVSMLFTSIAK-LTPEAANPFFKLLTMLMEFAGGPPgmppfasyilqRIWEVIEYNPSQC--------- 2680
Cdd:pfam12030 224 LLWENPELSDSILKTLLWGIRGaPAHLLRDPFLRAAIVFCEDSWQAH-----------RIHNLIDHVAKQAdslnntegr 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2681 --LDWL--AVQTPRNKL------AHSWVLQNMENWVErFLLAHNYPRVRTSAAYLLVSLI 2730
Cdd:pfam12030 293 afLHFFkrAYQCINCRLgfdkewFASQVLENIPDWAP-PLLSYPDSNVRSETEDFLQEEL 351
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1933-2274 |
1.24e-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: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1933 GLTNLGATCYLASTIQQLYMIPearqavftakysedmkhkttllelqkmftYLMEseckaynprpFCKTYTmdkqplntg 2012
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP-----------------------------SLIE----------YLEEFL--------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2013 EQKDMTEFFTDLITKVEemspelkNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEvtiKDTL 2092
Cdd:cd02662 33 EQQDAHELFQVLLETLE-------QLLKFPFDGLLASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTL---EHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2093 EGDNM------YTCSHCgkkvraekRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDmtpytedflmgksd 2166
Cdd:cd02662 103 DDFLSteiiddYKCDRC--------QTVIVRLPQILCIHLSRSVFDG-RGTSTKNSCKVSFPERLP-------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2167 rkegfkdvgdrskdteSYEYDLIGVTVHTGTADGGHYYSFIR-----------DIVNPHAYKN---NKWYLFNDAEVKpf 2232
Cdd:cd02662 160 ----------------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepgSFVRMREGPSstsHPWWRISDTTVK-- 221
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568969975 2233 dsaqlasECfggemttKTYDSVTDKfmdfsfekthSAYMLFY 2274
Cdd:cd02662 222 -------EV-------SESEVLEQK----------SAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1932-2229 |
1.26e-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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1932 VGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYS----EDMKHKTTLL------------------ELQKMFTYLMESE 1989
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaelASDYPTERRIggrevsrselqrsnqfvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 1990 CKAYNPRPFCKTYTMDKQplNTGEQKDMTEFFTDLITK---VEEMSPELKNT------VKSLFGG--------VITNNVV 2052
Cdd:cd02666 82 TRSVTPSKELAYLALRQQ--DVTECIDNVLFQLEVALEpisNAFAGPDTEDDkeqsdlIKRLFSGktkqqlvpESMGNQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2053 SLDC--EHVSQTA----EEFYTVRCQvADMKNIYESLDEVtikdtLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNT 2126
Cdd:cd02666 160 SVRTktERFLSLLvdvgKKGREIVVL-LEPKDLYDALDRY-----FDYDSLTKLPQRSQVQAQLAQPLQRELISMDRYEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2127 MRYTFNMVTMMKEKVNTHFSfplRLDMTPYTEDFLmgKSDRKEGFKDVgdrskdtESYEYDLIGVTVHTGTADGGHYYSF 2206
Cdd:cd02666 234 PSSIDDIDELIREAIQSESS---LVRQAQNELAEL--KHEIEKQFDDL-------KSYGYRLHAVFIHRGEASSGHYWVY 301
|
330 340
....*....|....*....|...
gi 568969975 2207 IRDivnphaYKNNKWYLFNDAEV 2229
Cdd:cd02666 302 IKD------FEENVWRKYNDETV 318
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2013-2275 |
6.85e-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: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2013 EQKDMTEFFTDLITKVEEMSPELKntvkslfggvitnnvvsLDCEHVSQTAEEfytvrcqvaDMKNIYESLDEVTIKDTl 2092
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEPK-----------------VDIIHGGKKDQD---------DDKLVNERLLQIPVPDD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2093 EGDNMYTCSHCGKkvRAEKRACFKKLPRILSFNTMRYTfnMVTMMKEKVNTHFSFPLRLDMTPYTED----FLMGKSDRK 2168
Cdd:cd02670 75 DDGGGITLEQCLE--QYFNNSVFAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDIPDFVADdpraCSKCQLECR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2169 EGFKDVgDRSKDTESYEYDLIGVTVHTGTA-DGGHYYSFIR-----DIVNPHAYKNNKWYLFndaevkpfDSAQLASECF 2242
Cdd:cd02670 151 VCYDDK-DFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVRygsysLTETDNEAYNAQWVFF--------DDMADRDGVS 221
|
250 260 270
....*....|....*....|....*....|...
gi 568969975 2243 GGemttktyDSVTDKFmdfsfeKTHSAYMLFYK 2275
Cdd:cd02670 222 NG-------FNIPAAR------LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2108-2233 |
8.93e-04 |
|
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: 44.04 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969975 2108 RAEKRACFKKLPRILSFNTMRYtfNMVTMMKEKVNTHFSFPLRLDMTPYTEDF--LMGKSDRKEGFKDVGDRSKDTES-Y 2184
Cdd:cd02672 134 KAWCDTCCKYQPLEQTTSIRHL--PDILLLVLVINLSVTNGEFDDINVVLPSGkvMQNKVSPKAIDHDKLVKNRGQESiY 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568969975 2185 EYDLIGVTVHTGTAD-GGHYYSFIRDIvnPHAYKNNKWYLFNDAEVKPFD 2233
Cdd:cd02672 212 KYELVGYVCEINDSSrGQHNVVFVIKV--NEESTHGRWYLFNDFLVTPVS 259
|
|
| |
