|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1892-2241 |
2.12e-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: 493.70 E-value: 2.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1892 RFVGLTNLGATCYLASTIQQLYMIPEARQAVFT---AKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPfcKTYTMDK 1968
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTD--KTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1969 QPLNTGEQKDMTEFFTDLITKIEEMSP--ELKNTVKSLFGGVITNNVVSLDCEHVSqtAEEFYTVRCQVADM--KNIYES 2044
Cdd:cd02659 79 DSLNTFEQHDVQEFFRVLFDKLEEKLKgtGQEGLIKNLFGGKLVNYIICKECPHES--EREEYFLDLQVAVKgkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2045 LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLM 2124
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2125 GkserkegfKEVSDHSKDSESYEYDLIGVTVHTGTADGGHYYSFIRDIVnphaykNNKWYLFNDAEVKPFDSAQLASECF 2204
Cdd:cd02659 237 K--------KEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPNDAEEECF 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 110347427 2205 GGEMTTKTYDSVtdkfmDFSFEKTHSAYMLFYKRMEP 2241
Cdd:cd02659 303 GGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1894-2236 |
3.05e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 213.84 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1894 VGLTNLGATCYLASTIQQLYMIPEARQAVF----TAKYSEDMKHKTTLLELQKMFTYL-MESECKAYNPRPFCKTYTMDK 1968
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLrispLSEDSRYNKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1969 QPLNTGEQKDMTEFFTDLITKIEE-MSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKN--- 2040
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEdLNGnhstENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2041 ---IYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPLRLDMTP 2117
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2118 YTEdflmgkserkEGFKEvsdhsKDSESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPfdsa 2197
Cdd:pfam00443 239 YLA----------EELKP-----KTNNLQDYRLVAVVVHSGSLSSGHYIAYIK------AYENNRWYKFDDEKVTE---- 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 110347427 2198 qlasecfggemttktydsVTDKFMdfsfEKTHSAYMLFY 2236
Cdd:pfam00443 294 ------------------VDEETA----VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1895-2237 |
9.96e-56 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 195.78 E-value: 9.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplntg 1974
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1975 EQKDMTEFFTDLITKIEEM----------SPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KN 2040
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEElkksskrtsdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKglpqVS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2041 IYESLDEVTIKDTLEGDNMYTCSHCgKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDMTPYTE 2120
Cdd:cd02257 101 LEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2121 DflmgkserkegfkEVSDHSKDSESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphayKNNKWYLFNDAEVKPfdsaql 2199
Cdd:cd02257 179 E-------------GEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDP------SDGKWYKFNDDKVTE------ 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 110347427 2200 asecfggemttktydsVTDKFMDFSFEKTHSAYMLFYK 2237
Cdd:cd02257 234 ----------------VSEEEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2237 |
3.88e-55 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 196.49 E-value: 3.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHK-----------TTLLELQKMFTYLMESECKAYNPRPFCKT 1963
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKnmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1964 YTmdkqpLNTGEQKDMTEFFTDLITKIE-----EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM 2038
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEaklskSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2039 KNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPY 2118
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2119 TEDflmgkserkegfkevsdhsKDSESYEYDLIGVTVHTGT-ADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSA 2197
Cdd:cd02668 236 LAE-------------------SDEGSYVYELSGVLIHQGVsAYSGHYIAHIKD------EQTGEWYKFNDEDVEEMPGK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 110347427 2198 QLasECFGGEMTTKTYDSVTDKfmdfSFEKTHSAYMLFYK 2237
Cdd:cd02668 291 PL--KLGNSEDPAKPRKSEIKK----GTHSSRTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2236 |
3.24e-40 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 152.82 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKT--TLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLN 1972
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1973 TGEQKDMTEFFTDLITKIE-----------EMSPELKNT--VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK 2039
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMQkacldrfkklkAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2040 NIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMmkEKVNTHFSFPLRLDMTPYt 2119
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RG--GKINKQISFPETLDLSPY- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2120 edflmgkserkegfkeVSDhsKDSESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphaykNNKWYLFNDAEVKPFDSAQ 2198
Cdd:cd02661 238 ----------------MSQ--PNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSS-------NGKWYNMDDSKVSPVSIET 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 110347427 2199 LASEcfggemttktydsvtdkfmdfsfekthSAYMLFY 2236
Cdd:cd02661 293 VLSQ---------------------------KAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1879-2244 |
1.01e-36 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 153.49 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1879 WDYWPHEDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFtYLMESECKAYNPR 1958
Cdd:COG5077 179 WHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLF-YNLQTGEEPVDTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1959 PFCKTYTMDKqpLNTGEQKDMTEFFTDLITKIEE--MSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA 2036
Cdd:COG5077 258 ELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKsmRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2037 DMKNIYESLDEVTIKDTLEGDNMYTCSHCGkKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMT 2116
Cdd:COG5077 336 GMKNLQESFRRYIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2117 PytedFLMGKSERKEgfkevsdhskdSESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPFDS 2196
Cdd:COG5077 415 P----FLDRDADKSE-----------NSDAVYVLYGVLVHSGDLHEGHYYALLK------PEKDGRWYKFDDTRVTRATE 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 110347427 2197 AQLASECFGGEMTTKtydsvtDKFMDFSFEKTH-SAYMLFYKRMEPEEE 2244
Cdd:COG5077 474 KEVLEENFGGDHPYK------DKIRDHSGIKRFmSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2204 |
8.40e-36 |
|
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: 140.59 E-value: 8.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLL----ELQKMFTYLMESEckayNPRPFCKTYTM---- 1966
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSclscAMDEIFQEFYYSG----DRSPYGPINLLylsw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1967 -DKQPLNTGEQKDMTEFFTDLITKIEEMS---PELKNTVKS-------LFGGVITNNVVSLDCEHVSQTAEEF------- 2028
Cdd:cd02660 78 kHSRNLAGYSQQDAHEFFQFLLDQLHTHYggdKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFldlsldi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2029 --------YTVRCQVADMKNIYESLDEVTIKDTLeGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMK 2100
Cdd:cd02660 158 pnkstpswALGESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL-NKTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2101 EKVNTHFSFPLRLDMTPYTedflmgkserKEGFKEVSDHSKDSESYEYDLIGVTVHTGTADGGHYYSFIRdivnphaYKN 2180
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYT----------SSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCR-------QGD 298
|
330 340
....*....|....*....|....*
gi 110347427 2181 NKWYLFNDAEVKPFDSAQ-LASECF 2204
Cdd:cd02660 299 GQWFKFDDAMITRVSEEEvLKSQAY 323
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2237 |
2.29e-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: 121.63 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLymipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplnTG 1974
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------------------------------------------------SA 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1975 EQKDMTEFFTDLITKIEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK------NIYESLDEV 2048
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHSI-------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLF 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2049 TIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPLR-LDMTPYTEDflmgkS 2127
Cdd:cd02674 94 TKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR--FSFSRGSTRKLTTPVTFPLNdLDLTPYVDT-----R 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2128 ERKEGFKevsdhskdsesyeYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPfdsaqlasecfgge 2207
Cdd:cd02674 167 SFTGPFK-------------YDLYAVVNHYGSLNGGHYTAYCKN------NETNDWYKFDDSRVTK-------------- 213
|
330 340 350
....*....|....*....|....*....|
gi 110347427 2208 mttktydsvtdkfMDFSFEKTHSAYMLFYK 2237
Cdd:cd02674 214 -------------VSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2237 |
3.15e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 115.67 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNP--------RPfcktytm 1966
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpdyfleasRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1967 dkQPLNTGEQKDMTEFFTDLITKieemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVR---CQVADMKNIYE 2043
Cdd:cd02664 74 --PWFTPGSQQDCSEYLRYLLDR-------LHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDlsfPSVQDLLNYFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2044 SldevtiKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFL 2123
Cdd:cd02664 145 S------PEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2124 MGKSERKEGFKEVSDHSKDSESYEYDLIGVTVHTGTA-DGGHYYSFIRDIVN----------PHAYKNNK----WYLFND 2188
Cdd:cd02664 219 SESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpePKDAEENDesknWYLFND 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 110347427 2189 AEVkpfdsaqlaSECfggemTTKTYDSVTdkfmdfSFEKTHSAYMLFYK 2237
Cdd:cd02664 299 SRV---------TFS-----SFESVQNVT------SRFPKDTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2171 |
2.19e-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: 105.93 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPeARQAVFtakySEDMKhkttllelqKMFtylmeSECKAYNPRpfcktytmdkqpLNTG 1974
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP-ALRELL----SETPK---------ELF-----SQVCRKAPQ------------FKGY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1975 EQKDMTEFFTDLITKieemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KNIYESLDEVTI 2050
Cdd:cd02667 50 QQQDSHELLRYLLDG-------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEikseCSIESCLKQFTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2051 KDTLEGDNMYTCSHCgkkVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKeKVNTHFSFPLRLDMTPytedFLMGKSErk 2130
Cdd:cd02667 123 VEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAP----FCDPKCN-- 192
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 110347427 2131 egfkevsdHSKDSESYEYDLIGVTVHTGTADGGHYYSFIRD 2171
Cdd:cd02667 193 --------SSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2237 |
9.01e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 104.70 E-value: 9.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYmipearqavftakysedmkHKTTLLELQKMFTYLMESECK--AYNPRPFCKTYTMDKQPLN 1972
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRtgVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1973 TGEQKDMTEFFTDLITKI------------------EEMSPELKNT-VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRC 2033
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIaeildaerkaekanrklnNNNNAEPQPTwVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2034 QVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRL 2113
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2114 DMtpytedflmgkserkegfKEVSDHSKDSESyEYDLIGVTVHTG-TADGGHYYSFIRdivnphayKNNKWYLFNDAEVK 2192
Cdd:cd02663 222 RL------------------FNTTDDAENPDR-LYELVAVVVHIGgGPNHGHYVSIVK--------SHGGWLLFDDETVE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110347427 2193 PFDSAQLAsECFGGEMTTKTydsvtdkfmdfsfekthsAYMLFYK 2237
Cdd:cd02663 275 KIDENAVE-EFFGDSPNQAT------------------AYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2237 |
1.90e-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: 103.95 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPEARQAV--FTAKYSEDMKHKTTLL-ELQKMFTyLMESECKAYNPRPFCKTYTM----- 1966
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQSSDNLTnALRDLFD-TMDKKQEPVPPIEFLQLLRMafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1967 -DKQPLNTGEQKDMTEFFTDLITKIE---EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQ-TAEEFYTVRCQVaDMKNI 2041
Cdd:cd02657 80 aEKQNQGGYAQQDAEECWSQLLSVLSqklPGAGSKGSFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHI-SITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2042 YESLDEvTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTpyteD 2121
Cdd:cd02657 159 VNYLQD-GLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY----E 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2122 FLmgkserkegfkevsdhskdSESYEYDLIGVTVHTG-TADGGHYYSFIRDivnphaYKNNKWYLFNDA---EVKPFDSA 2197
Cdd:cd02657 234 LC-------------------TPSGYYELVAVITHQGrSADSGHYVAWVRR------KNDGKWIKFDDDkvsEVTEEDIL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 110347427 2198 QLASecfGGEmttktydsvtdkfmdfsfekTHSAYMLFYK 2237
Cdd:cd02657 289 KLSG---GGD--------------------WHIAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2191 |
2.71e-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: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPEARQAVFT--AKYSEDMKHKTTLLELQ--KMFT------YLMESECKAYN-------- 1956
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVDPANDLNCQliKLADgllsgrYSKPASLKSENdpyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1957 PRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKIE-EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQV 2035
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDrESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2036 ADMKNIYESLDE-----VTIKDTLEG-----DNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvtmmKEKVnt 2105
Cdd:cd02658 161 PKDEATEKEEGElvyepVPLEDCLKAyfapeTIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL-----ENWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2106 hfsfPLRLDMTPYTEDFLMGKserkegfkevsdhskdsesyEYDLIGVTVHTGT-ADGGHYYSFIRDIVNPhaykNNKWY 2184
Cdd:cd02658 234 ----PKKLDVPIDVPEELGPG--------------------KYELIAFISHKGTsVHSGHYVAHIKKEIDG----EGKWV 285
|
....*..
gi 110347427 2185 LFNDAEV 2191
Cdd:cd02658 286 LFNDEKV 292
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1893-2192 |
1.12e-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: 84.56 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1893 FVGLTNLGATCYLASTIQQLYMIPearqavftaKYSEDMKHKTTLL----ELQKMFTYLME---SECKAYNPRPFCKTyT 1965
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLIssveQLQSSFLLNPEkynDELANQAPRRLLNA-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1966 MDKQPLNTG-EQKDMTEFFTDLITKIEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA-DMKNIYE 2043
Cdd:cd02671 94 REVNPMYEGyLQHDAQEVLQCILGNIQEL-------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQeSELSKSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2044 SLDEVTIKDTLE------------------GDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMK----E 2101
Cdd:cd02671 167 ESSEISPDPKTEmktlkwaisqfasverivGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCygglS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2102 KVNTHFSFPLRLDmtpytedfLMGKSERKegfkevsdhskdsESYEYDLIGVTVHTG-TADGGHYYSFIRdivnphaykn 2180
Cdd:cd02671 247 KVNTPLLTPLKLS--------LEEWSTKP-------------KNDVYRLFAVVMHSGaTISSGHYTAYVR---------- 295
|
330
....*....|..
gi 110347427 2181 nkWYLFNDAEVK 2192
Cdd:cd02671 296 --WLLFDDSEVK 305
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1894-2188 |
1.62e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 83.47 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1894 VGLTNLGATCYLASTIQQLYMIPEARQ-AVFTAKySEDMKHKTTLLELQKMFTYLMESE---CKAYNprpFCKTYT---- 1965
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLA-TECLKEHCLLCELGFLFDMLEKAKgknCQASN---FLRALSsipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1966 ------MDKQPLNTGEQKDMT------EFFTDLITKIEEMSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFY 2029
Cdd:pfam13423 77 asalglLDEDRETNSAISLSSliqsfnRFLLDQLSSEENSTPpnpsPAESPLEQLFGIDAETTIRCSNCGHESVRESSTH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2030 TVRCQVADMKNIYESLDEVT-----IKDTLEGDNMY--TCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVtmmKEK 2102
Cdd:pfam13423 157 VLDLIYPRKPSSNNKKPPNQtfssiLKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWR---QLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2103 VNTHFsFPLRLDMTPYTedflmgkserkegfkevsDHSKDSESYEYDLIGVTVHTGTADG-GHYYSFIR-DIVNPHAYKN 2180
Cdd:pfam13423 234 KTPGW-LPPEIGLTLSD------------------DLQGDNEIVKYELRGVVVHIGDSGTsGHLVSFVKvADSELEDPTE 294
|
....*...
gi 110347427 2181 NKWYLFND 2188
Cdd:pfam13423 295 SQWYLFND 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1895-2238 |
3.61e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.08 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQL---------YMIPEARQA-VFTAKYSEDMKHKTtLLELQKMFTYLMESECKAYNPRPfckty 1964
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldeLLDDLSKELkVLKNVIRKPEPDLN-QEEALKLFTALWSSKEHKVGWIP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1965 tmdkqplNTGEQKDMTEFFTDLItkiEEMSPELKNTVKSLFGGVITNNVVSLDCE----HVS----QTAEEFYTVRCQVA 2036
Cdd:COG5533 75 -------PMGSQEDAHELLGKLL---DELKLDLVNSFTIRIFKTTKDKKKTSTGDwfdiIIElpdqTWVNNLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2037 DMKniYESLDEVTIKdtlEGDNMytcshcGKKVRA--EKRACFKKLPRILSFNTMRYTF-NMVTMMKEKVNTHFSFPLRL 2113
Cdd:COG5533 145 NME--ELVDDETGVK---AKENE------ELEVQAkqEYEVSFVKLPKILTIQLKRFANlGGNQKIDTEVDEKFELPVKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2114 DmtpytedflmgkserkegfkevsDHSKDSESYEYDLIGVTVHTGTADGGHYYSFIRdivnphayKNNKWYLFNDAEVKP 2193
Cdd:COG5533 214 D-----------------------QILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--------KGGKWEKANDSDVTP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110347427 2194 FDSaqlasecfggemtTKTYDsvtdkfmdfsfEKTHSAYMLFYKR 2238
Cdd:COG5533 263 VSE-------------EEAIN-----------EKAKNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1893-2192 |
2.15e-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: 69.27 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1893 FVGLTNLGATCYLASTIQQLYMIPEARQavFTAKYSEDMKHKTTLLELQKMFTYLMEsecKAYNPRPFcKTY-------- 1964
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRN--FFLLYENYENIKDRKSELVKRLSELIR---KIWNPRNF-KGHvsphellq 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1965 ---TMDKQPLNTGEQKDMTEFFTDLITKI----EEMSPELKNTVKSLFGGVITN-----NVVSLDCEHVSQTAEEFYTVr 2032
Cdd:cd02669 193 avsKVSKKKFSITEQSDPVEFLSWLLNTLhkdlGGSKKPNSSIIHDCFQGKVQIetqkiKPHAEEEGSKDKFFKDSRVK- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2033 cQVADMKNIYESLD-----------------EVTIKDTLEGDNMYTCSHCGKKVraeKRACFKKLPRILSFNTMRYTFNm 2095
Cdd:cd02669 272 -KTSVSPFLLLTLDlpppplfkdgneeniipQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSKN- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2096 vTMMKEKVNTHFSFPLR-LDMTPYTEdflmgkserkegfkevSDHSKDSESYEYDLIGVTVHTGT-ADGGHYYSFIRDiv 2173
Cdd:cd02669 347 -NFFKEKNPTIVNFPIKnLDLSDYVH----------------FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRH-- 407
|
330
....*....|....*....
gi 110347427 2174 nphaYKNNKWYLFNDAEVK 2192
Cdd:cd02669 408 ----KSTNKWFEIQDLNVK 422
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2206 |
7.75e-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: 64.89 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYmipearqavftaKYSEDMKHKTTLLelqkmFTYLMES-ECKAYNPRPfcktytmDKQPLNt 1973
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF------------SQQQDVSEFTHLL-----LDWLEDAfQAAAEAISP-------GEKSKN- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1974 geqkDMTEFFTdlitkieemspELKNTVKSLFGGVITNNvvsldcehvsqtaEEFYTVRCQVADMKNIYESLDEVTIKDT 2053
Cdd:cd02665 56 ----PMVQLFY-----------GTFLTEGVLEGKPFCNC-------------ETFGQYPLQVNGYGNLHECLEAAMFEGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2054 LEGDnmytcsHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPLRLDMTPYtedflmgkserkegf 2133
Cdd:cd02665 108 VELL------PSDHSVKSGQERWFTELPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQVPY--------------- 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347427 2134 kevsdhskdsesyeyDLIGVTVHTGTADGGHYYSFIRDivNPHayknNKWYLFNDAEVKPFDSAQLASECFGG 2206
Cdd:cd02665 165 ---------------ELHAVLVHEGQANAGHYWAYIYK--QSR----QEWEKYNDISVTESSWEEVERDSFGG 216
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1982-2238 |
2.60e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 66.83 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1982 FFTDLITKIEemSPELKNTVKSlfGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYES--------LDEVTIKDT 2053
Cdd:COG5560 614 SWLKLETEID--TKREEQVEEE--GQMNFNDAVVISCEWEEKRYLSLFSYDPLWTIREIGAAErtitlqdcLNEFSKPEQ 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2054 LEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPL-RLDMTPYTedflmgkserkeg 2132
Cdd:COG5560 690 LGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIdDLDLSGVE------------- 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2133 fkevsdHSKDSESYEYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSAqlasecfggemttkt 2212
Cdd:COG5560 755 ------YMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARN------FANNGWYLFDDSRITEVDPE--------------- 807
|
250 260
....*....|....*....|....*.
gi 110347427 2213 yDSVTDkfmdfsfekthSAYMLFYKR 2238
Cdd:COG5560 808 -DSVTS-----------SAYVLFYRR 821
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2359-2692 |
1.39e-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: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2359 QILIKCPNQIVRQMFQRLCIHVIQRLrpvHAHLYLQPGMEDGSDDMDTsvEDIGGRSCVTRFVRTLLLIMEHgVKPHSKH 2438
Cdd:pfam12030 6 ELLLRNPDAEVRSAFGKLIVFALHKL---KELYGLPDGPCDPDDLEEE--WRSLSDSVLEAVVALLDHLWKE-FHTHLRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2439 LTEYFAFLYEFAKMGEEESQFLLS---LQAISTMVHFYMGTKGPENPQ-VEVLSEEegeeeeeeedilslaeEKYRPAAL 2514
Cdd:pfam12030 80 WDEYFGLLLSYANLGPREVAQLLDlgfLLKCLEIIAADEGDGPPLKYQyARMLRLV----------------EKRRPPSY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2515 EKMIALVALLVEQSRSERHLTLSQT---DMAALTGGKGFPF------LFQH-------------IRDGINIRQTCNLIFS 2572
Cdd:pfam12030 144 EKLIQLLSVLLRCCDLSLPPQSINEgaePLPNSLPDGPFPLtseeadLLRPlgrtngsifvkklLEIDQNPEATRKILRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2573 LCRYNNRLAEHIVSMLFTSIAK-LTPEAANPFFKLLTMLMEFAGGPPgmppfasyilqRIWEVIEYNPSQC--------- 2642
Cdd:pfam12030 224 LLWENPELSDSILKTLLWGIRGaPAHLLRDPFLRAAIVFCEDSWQAH-----------RIHNLIDHVAKQAdslnntegr 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2643 --LDWL--AVQTPRNKL------AHSWVLQNMENWVErFLLAHNYPRVRTSAAYLLVSLI 2692
Cdd:pfam12030 293 afLHFFkrAYQCINCRLgfdkewFASQVLENIPDWAP-PLLSYPDSNVRSETEDFLQEEL 351
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1895-2236 |
1.71e-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: 55.06 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1895 GLTNLGATCYLASTIQQLYMIPearqavftakysedmkhkttllelqkmftYLMEseckaynprpFCKTYTmdkqplntg 1974
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP-----------------------------SLIE----------YLEEFL--------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1975 EQKDMTEFFTDLITKIEemspelkNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEvtiKDTL 2054
Cdd:cd02662 33 EQQDAHELFQVLLETLE-------QLLKFPFDGLLASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTL---EHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2055 EGDNM------YTCSHCgkkvraekRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDmtpytedflmgkse 2128
Cdd:cd02662 103 DDFLSteiiddYKCDRC--------QTVIVRLPQILCIHLSRSVFDG-RGTSTKNSCKVSFPERLP-------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2129 rkegfkevsdhskdseSYEYDLIGVTVHTGTADGGHYYSFIR-----------DIVNPHAYKN---NKWYLFNDAEVKpf 2194
Cdd:cd02662 160 ----------------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepgSFVRMREGPSstsHPWWRISDTTVK-- 221
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110347427 2195 dsaqlasECfggemttKTYDSVTDKfmdfsfekthSAYMLFY 2236
Cdd:cd02662 222 -------EV-------SESEVLEQK----------SAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1894-2191 |
3.65e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 52.11 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1894 VGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYS----EDMKHKTTLL------------------ELQKMFTYLMESE 1951
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaelASDYPTERRIggrevsrselqrsnqfvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1952 CKAYNPRPFCKTYTMDKQplNTGEQKDMTEFFTDLITKIEEMSP---------ELKNTVKSLFGG--------VITNNVV 2014
Cdd:cd02666 82 TRSVTPSKELAYLALRQQ--DVTECIDNVLFQLEVALEPISNAFagpdteddkEQSDLIKRLFSGktkqqlvpESMGNQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2015 SLDC--EHVSQTA----EEFYTVRCQvADMKNIYESLDEVTIKDTLEgdnmytcshcgkKVRAEKRacfkkLPRILSFNT 2088
Cdd:cd02666 160 SVRTktERFLSLLvdvgKKGREIVVL-LEPKDLYDALDRYFDYDSLT------------KLPQRSQ-----VQAQLAQPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2089 MRYTFNMVTM-MKEKVNTHFSFpLRLDMTPYTEDFLMGKSERKEGFKEVSDHSKDSESYEYDLIGVTVHTGTADGGHYYS 2167
Cdd:cd02666 222 QRELISMDRYeLPSSIDDIDEL-IREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWV 300
|
330 340
....*....|....*....|....
gi 110347427 2168 FIRDivnphaYKNNKWYLFNDAEV 2191
Cdd:cd02666 301 YIKD------FEENVWRKYNDETV 318
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1975-2237 |
1.29e-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: 49.45 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 1975 EQKDMTEFFTDLITKIEEMSPELKntvkslfggvitnnvvsLDCEHVSQTAEEfytvrcqvaDMKNIYESLDEVTIKDTl 2054
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEPK-----------------VDIIHGGKKDQD---------DDKLVNERLLQIPVPDD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2055 EGDNMYTCSHCGKkvRAEKRACFKKLPRILSFNTMRYTfnMVTMMKEKVNTHFSFPLRLDMTPYTED----FLMGKSERK 2130
Cdd:cd02670 75 DDGGGITLEQCLE--QYFNNSVFAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDIPDFVADdpraCSKCQLECR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2131 EGFKEVSDhSKDSESYEYDLIGVTVHTGTA-DGGHYYSFIR-----DIVNPHAYKNNKWYLFndaevkpfDSAQLASECF 2204
Cdd:cd02670 151 VCYDDKDF-SPTCGKFKLSLCSAVCHRGTSlETGHYVAFVRygsysLTETDNEAYNAQWVFF--------DDMADRDGVS 221
|
250 260 270
....*....|....*....|....*....|...
gi 110347427 2205 GGemttktyDSVTDKFmdfsfeKTHSAYMLFYK 2237
Cdd:cd02670 222 NG-------FNIPAAR------LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2070-2195 |
2.84e-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: 42.50 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347427 2070 RAEKRACFKKLPRILSFNTMRYtfNMVTMMKEKVNTHFSFPLRLDMTPYTEDF--LMGKSERKEGFKEVSDHSKDSES-Y 2146
Cdd:cd02672 134 KAWCDTCCKYQPLEQTTSIRHL--PDILLLVLVINLSVTNGEFDDINVVLPSGkvMQNKVSPKAIDHDKLVKNRGQESiY 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 110347427 2147 EYDLIGVTVHTGTAD-GGHYYSFIRDIvnPHAYKNNKWYLFNDAEVKPFD 2195
Cdd:cd02672 212 KYELVGYVCEINDSSrGQHNVVFVIKV--NEESTHGRWYLFNDFLVTPVS 259
|
|
| |
