|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1918-2267 |
4.12e-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: 492.93 E-value: 4.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1918 RFVGLTNLGATCYLASTIQQLYMIPEARQAVFT---AKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPfcKTYTMDK 1994
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTD--KTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1995 QPLNTGEQKDMTEFFTDLITKVEEMSP--ELKNTVKSLFGGVITNNVVSLDCEHVSqtAEEFYTVRCQVADM--KNIYES 2070
Cdd:cd02659 79 DSLNTFEQHDVQEFFRVLFDKLEEKLKgtGQEGLIKNLFGGKLVNYIICKECPHES--EREEYFLDLQVAVKgkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2071 LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLM 2150
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2151 GksdrkegfKDVGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRDIVnphaykNNKWYLFNDAEVKPFDSAQLASECF 2230
Cdd:cd02659 237 K--------KEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPNDAEEECF 302
|
330 340 350
....*....|....*....|....*....|....*..
gi 568969977 2231 GGEMTTKTYDSVtdkfmDFSFEKTHSAYMLFYKRMEP 2267
Cdd:cd02659 303 GGEETQKTYDSG-----PRAFKRTTNAYMLFYERKSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1920-2262 |
1.88e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 214.23 E-value: 1.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1920 VGLTNLGATCYLASTIQQLYMIPEARQAVF----TAKYSEDMKHKTTLLELQKMFTYL-MESECKAYNPRPFCKTYTMDK 1994
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLrispLSEDSRYNKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1995 QPLNTGEQKDMTEFFTDLITKVEE-MSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKN--- 2066
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEdLNGnhstENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2067 ---IYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPLRLDMTP 2143
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2144 YTEDflmgksdrkegfkdvGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPfdsa 2223
Cdd:pfam00443 239 YLAE---------------ELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK------AYENNRWYKFDDEKVTE---- 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 568969977 2224 qlasecfggemttktydsVTDKFMdfsfEKTHSAYMLFY 2262
Cdd:pfam00443 294 ------------------VDEETA----VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1921-2263 |
1.42e-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: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplntg 2000
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2001 EQKDMTEFFTDLITKVEEM----------SPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KN 2066
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEElkksskrtsdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKglpqVS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2067 IYESLDEVTIKDTLEGDNMYTCSHCgKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDMTPYTE 2146
Cdd:cd02257 101 LEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2147 DFLMgksdrkegfkdvgDRSKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphayKNNKWYLFNDAEVKPfdsaql 2225
Cdd:cd02257 179 EGEK-------------DSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDP------SDGKWYKFNDDKVTE------ 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 568969977 2226 asecfggemttktydsVTDKFMDFSFEKTHSAYMLFYK 2263
Cdd:cd02257 234 ----------------VSEEEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2263 |
1.02e-54 |
|
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: 1.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHK-----------TTLLELQKMFTYLMESECKAYNPRPFCKT 1989
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKnmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1990 YTmdkqpLNTGEQKDMTEFFTDLITKVE-----EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM 2064
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEaklskSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2065 KNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPY 2144
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2145 TEDflmgksdrkegfkdvgdrsKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSA 2223
Cdd:cd02668 236 LAE-------------------SDEGSYVYELSGVLIHQGVsAYSGHYIAHIKD------EQTGEWYKFNDEDVEEMPGK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568969977 2224 QLasECFGGEMTTKTYDSVTDKfmdfSFEKTHSAYMLFYK 2263
Cdd:cd02668 291 PL--KLGNSEDPAKPRKSEIKK----GTHSSRTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2262 |
2.43e-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: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKT--TLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLN 1998
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1999 TGEQKDMTEFFTDLITKVE-----------EMSPELKNT--VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK 2065
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMQkacldrfkklkAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2066 NIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMmkEKVNTHFSFPLRLDMTPYt 2145
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RG--GKINKQISFPETLDLSPY- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2146 edflMgkSDRKEGfkdvgdrskdteSYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphaykNNKWYLFNDAEVKPFDSAQ 2224
Cdd:cd02661 238 ----M--SQPNDG------------PLKYKLYAVLVHSGFsPHSGHYYCYVKSS-------NGKWYNMDDSKVSPVSIET 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 568969977 2225 LASEcfggemttktydsvtdkfmdfsfekthSAYMLFY 2262
Cdd:cd02661 293 VLSQ---------------------------KAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1905-2270 |
3.79e-37 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 154.64 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1905 WDYWPHEDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFtYLMESECKAYNPR 1984
Cdd:COG5077 179 WHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLF-YNLQTGEEPVDTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1985 PFCKTYTMDKqpLNTGEQKDMTEFFTDLITKVEE--MSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA 2062
Cdd:COG5077 258 ELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKsmRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2063 DMKNIYESLDEVTIKDTLEGDNMYTCSHCGkKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMT 2142
Cdd:COG5077 336 GMKNLQESFRRYIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2143 PytedFLMGKSDRKEgfkdvgdrSKDtesYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPFDS 2222
Cdd:COG5077 415 P----FLDRDADKSE--------NSD---AVYVLYGVLVHSGDLHEGHYYALLK------PEKDGRWYKFDDTRVTRATE 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568969977 2223 AQLASECFGGEMTTKtydsvtDKFMDFS-FEKTHSAYMLFYKRMEPEEE 2270
Cdd:COG5077 474 KEVLEENFGGDHPYK------DKIRDHSgIKRFMSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2230 |
5.40e-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: 138.27 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLL----ELQKMFTYLMESEckayNPRPFCKTYTM---- 1992
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSclscAMDEIFQEFYYSG----DRSPYGPINLLylsw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1993 -DKQPLNTGEQKDMTEFFTDLITKVEEMS---PELKNTVKS-------LFGGVITNNVVSLDCEHVSQTAEEF------- 2054
Cdd:cd02660 78 kHSRNLAGYSQQDAHEFFQFLLDQLHTHYggdKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFldlsldi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2055 --------YTVRCQVADMKNIYESLDEVTIKDTLeGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMK 2126
Cdd:cd02660 158 pnkstpswALGESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL-NKTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2127 EKVNTHFSFPLRLDMTPYTedflmgksdrKEGFKDVGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRdivnphaYKN 2206
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYT----------SSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCR-------QGD 298
|
330 340
....*....|....*....|....*
gi 568969977 2207 NKWYLFNDAEVKPFDSAQ-LASECF 2230
Cdd:cd02660 299 GQWFKFDDAMITRVSEEEvLKSQAY 323
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2263 |
1.87e-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: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLymipearqavftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplnTG 2000
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------------------------------------------------SA 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2001 EQKDMTEFFTDLITkveemspELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK------NIYESLDEV 2074
Cdd:cd02674 21 DQQDAQEFLLFLLD-------GLHSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLF 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2075 TIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPLR-LDMTPYTEDflmgkS 2153
Cdd:cd02674 94 TKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR--FSFSRGSTRKLTTPVTFPLNdLDLTPYVDT-----R 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2154 DRKEGFKdvgdrskdtesyeYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPfdsaqlasecfgge 2233
Cdd:cd02674 167 SFTGPFK-------------YDLYAVVNHYGSLNGGHYTAYCKN------NETNDWYKFDDSRVTK-------------- 213
|
330 340 350
....*....|....*....|....*....|
gi 568969977 2234 mttktydsvtdkfMDFSFEKTHSAYMLFYK 2263
Cdd:cd02674 214 -------------VSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2263 |
6.26e-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: 6.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNP--------RPfcktytm 1992
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpdyfleasRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1993 dkQPLNTGEQKDMTEFFTDLITKveemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVR---CQVADMKNIYE 2069
Cdd:cd02664 74 --PWFTPGSQQDCSEYLRYLLDR-------LHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDlsfPSVQDLLNYFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2070 SldevtiKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFL 2149
Cdd:cd02664 145 S------PEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2150 MGKSDRKEGFKDVGDRSKDTESYEYDLIGVTVHTGTA-DGGHYYSFIRDIVN----------PHAYKNNK----WYLFND 2214
Cdd:cd02664 219 SESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpePKDAEENDesknWYLFND 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568969977 2215 AEVkpfdsaqlaSECfggemTTKTYDSVTdkfmdfSFEKTHSAYMLFYK 2263
Cdd:cd02664 299 SRV---------TFS-----SFESVQNVT------SRFPKDTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2197 |
1.05e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 104.01 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPeARQAVFtakySEDMKhkttllelqKMFtylmeSECKAYNPRpfcktytmdkqpLNTG 2000
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP-ALRELL----SETPK---------ELF-----SQVCRKAPQ------------FKGY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2001 EQKDMTEFFTDLITKveemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KNIYESLDEVTI 2076
Cdd:cd02667 50 QQQDSHELLRYLLDG-------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEikseCSIESCLKQFTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2077 KDTLEGDNMYTCSHCgkkVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKeKVNTHFSFPLRLDMTPytedFLMGKSDRK 2156
Cdd:cd02667 123 VEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAP----FCDPKCNSS 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568969977 2157 EgfkdvgdrskDTESYEYDLIGVTVHTGTADGGHYYSFIRD 2197
Cdd:cd02667 195 E----------DKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2263 |
1.48e-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: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPEARQAV--FTAKYSEDMKHKTTLL-ELQKMFTyLMESECKAYNPRPFCKTYTM----- 1992
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQSSDNLTnALRDLFD-TMDKKQEPVPPIEFLQLLRMafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1993 -DKQPLNTGEQKDMTEFFTDLITKVE---EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQ-TAEEFYTVRCQVaDMKNI 2067
Cdd:cd02657 80 aEKQNQGGYAQQDAEECWSQLLSVLSqklPGAGSKGSFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHI-SITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2068 YESLDEvTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTpyteD 2147
Cdd:cd02657 159 VNYLQD-GLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY----E 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2148 FLmgksdrkegfkdvgdrskdTESYEYDLIGVTVHTG-TADGGHYYSFIRDivnphaYKNNKWYLFNDA---EVKPFDSA 2223
Cdd:cd02657 234 LC-------------------TPSGYYELVAVITHQGrSADSGHYVAWVRR------KNDGKWIKFDDDkvsEVTEEDIL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568969977 2224 QLASecfGGEmttktydsvtdkfmdfsfekTHSAYMLFYK 2263
Cdd:cd02657 289 KLSG---GGD--------------------WHIAYILLYK 305
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2263 |
2.44e-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: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYmipearqavftakysedmkHKTTLLELQKMFTYLMESECK--AYNPRPFCKTYTMDKQPLN 1998
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRtgVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1999 TGEQKDMTEFFTDLITKV------------------EEMSPELKNT-VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRC 2059
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIaeildaerkaekanrklnNNNNAEPQPTwVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2060 QVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRL 2139
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2140 DMTPYTEDflMGKSDRkegfkdvgdrskdtesyEYDLIGVTVHTG-TADGGHYYSFIRdivnphayKNNKWYLFNDAEVK 2218
Cdd:cd02663 222 RLFNTTDD--AENPDR-----------------LYELVAVVVHIGgGPNHGHYVSIVK--------SHGGWLLFDDETVE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568969977 2219 PFDSAQLAsECFGGEMTTKTydsvtdkfmdfsfekthsAYMLFYK 2263
Cdd:cd02663 275 KIDENAVE-EFFGDSPNQAT------------------AYVLFYQ 300
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2217 |
3.11e-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: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPEARQAVFT--AKYSEDMKHKTTLLELQ--KMFT------YLMESECKAYN-------- 1982
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVDPANDLNCQliKLADgllsgrYSKPASLKSENdpyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1983 PRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKVE-EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQV 2061
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDrESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2062 ADMKNIYESLDE-----VTIKDTLEG-----DNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvtmmKEKVnt 2131
Cdd:cd02658 161 PKDEATEKEEGElvyepVPLEDCLKAyfapeTIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL-----ENWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2132 hfsfPLRLDMTPYTEDFLMGKsdrkegfkdvgdrskdtesyEYDLIGVTVHTGT-ADGGHYYSFIRDIVNPhaykNNKWY 2210
Cdd:cd02658 234 ----PKKLDVPIDVPEELGPG--------------------KYELIAFISHKGTsVHSGHYVAHIKKEIDG----EGKWV 285
|
....*..
gi 568969977 2211 LFNDAEV 2217
Cdd:cd02658 286 LFNDEKV 292
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1919-2218 |
1.28e-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: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1919 FVGLTNLGATCYLASTIQQLYMIPearqavftaKYSEDMKHKTTLL----ELQKMFTYLME---SECKAYNPRPFCKTyT 1991
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLIssveQLQSSFLLNPEkynDELANQAPRRLLNA-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1992 MDKQPLNTG-EQKDMTEFFTDLITKVEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA-DMKNIYE 2069
Cdd:cd02671 94 REVNPMYEGyLQHDAQEVLQCILGNIQEL-------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQeSELSKSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2070 SLDEVTIKDTLE------------------GDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMK----E 2127
Cdd:cd02671 167 ESSEISPDPKTEmktlkwaisqfasverivGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCygglS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2128 KVNTHFSFPLRLDmtpytedfLMGKSDRKegfkdvgdrskdtESYEYDLIGVTVHTG-TADGGHYYSFIRdivnphaykn 2206
Cdd:cd02671 247 KVNTPLLTPLKLS--------LEEWSTKP-------------KNDVYRLFAVVMHSGaTISSGHYTAYVR---------- 295
|
330
....*....|..
gi 568969977 2207 nkWYLFNDAEVK 2218
Cdd:cd02671 296 --WLLFDDSEVK 305
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1920-2214 |
5.81e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 81.55 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1920 VGLTNLGATCYLASTIQQLYMIPEARQ-AVFTAKySEDMKHKTTLLELQKMFTYLMESE---CKAYNprpFCKTytMDKQ 1995
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLA-TECLKEHCLLCELGFLFDMLEKAKgknCQASN---FLRA--LSSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1996 P-------LNTGEQKDMTEFFTDLITK-----VEEMSPELK----------NTVKSLFGGVITNNVVSLDCEHVSQTAEE 2053
Cdd:pfam13423 75 PeasalglLDEDRETNSAISLSSLIQSfnrflLDQLSSEENstppnpspaeSPLEQLFGIDAETTIRCSNCGHESVRESS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2054 FYTVRCQVADMKNIYESLDEVT-----IKDTLEGDNMY--TCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVtmmK 2126
Cdd:pfam13423 155 THVLDLIYPRKPSSNNKKPPNQtfssiLKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWR---Q 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2127 EKVNTHFsFPLRLDMTPYTedflmgksdrkegfkdvgDRSKDTESYEYDLIGVTVHTGTADG-GHYYSFIR-DIVNPHAY 2204
Cdd:pfam13423 232 LWKTPGW-LPPEIGLTLSD------------------DLQGDNEIVKYELRGVVVHIGDSGTsGHLVSFVKvADSELEDP 292
|
330
....*....|
gi 568969977 2205 KNNKWYLFND 2214
Cdd:pfam13423 293 TESQWYLFND 302
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1921-2264 |
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 568969977 1921 GLTNLGATCYLASTIQQL---------YMIPEARQA-VFTAKYSEDMKHKTtLLELQKMFTYLMESECKAYNPRPfckty 1990
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldeLLDDLSKELkVLKNVIRKPEPDLN-QEEALKLFTALWSSKEHKVGWIP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1991 tmdkqplNTGEQKDMTEFFTDLItkvEEMSPELKNTVKSLFGGVITNNVVSLDCE----HVS----QTAEEFYTVRCQVA 2062
Cdd:COG5533 75 -------PMGSQEDAHELLGKLL---DELKLDLVNSFTIRIFKTTKDKKKTSTGDwfdiIIElpdqTWVNNLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2063 DMKniYESLDEVTIKdtlEGDNMytcshcGKKVRA--EKRACFKKLPRILSFNTMRYTF-NMVTMMKEKVNTHFSFPLRL 2139
Cdd:COG5533 145 NME--ELVDDETGVK---AKENE------ELEVQAkqEYEVSFVKLPKILTIQLKRFANlGGNQKIDTEVDEKFELPVKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2140 DMTpytedflmgKSDRKEGFkdvgdrskdtesyeYDLIGVTVHTGTADGGHYYSFIRdivnphayKNNKWYLFNDAEVKP 2219
Cdd:COG5533 214 DQI---------LNIVKETY--------------YDLVGFVLHQGSLEGGHYIAYVK--------KGGKWEKANDSDVTP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568969977 2220 FDSaqlasecfggemtTKTYDsvtdkfmdfsfEKTHSAYMLFYKR 2264
Cdd:COG5533 263 VSE-------------EEAIN-----------EKAKNAYLYFYER 283
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2232 |
4.88e-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: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYmipearqavftaKYSEDMKHKTTLLelqkmFTYLMES-ECKAYNPRPfcktytmDKQPLNt 1999
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF------------SQQQDVSEFTHLL-----LDWLEDAfQAAAEAISP-------GEKSKN- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2000 geqkDMTEFFTdlitkveemspELKNTVKSLFGGVITNNvvsldcehvsqtaEEFYTVRCQVADMKNIYESLDEVTIKDT 2079
Cdd:cd02665 56 ----PMVQLFY-----------GTFLTEGVLEGKPFCNC-------------ETFGQYPLQVNGYGNLHECLEAAMFEGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2080 LEGDnmytcsHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPlrldmtpytedflmgksdrkegf 2159
Cdd:cd02665 108 VELL------PSDHSVKSGQERWFTELPPVLTFELSRFEFN--QGRPEKIHDKLEFP----------------------- 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568969977 2160 kdvgdrsKDTESYEYDLIGVTVHTGTADGGHYYSFIRDivNPHayknNKWYLFNDAEVKPFDSAQLASECFGG 2232
Cdd:cd02665 157 -------QIIQQVPYELHAVLVHEGQANAGHYWAYIYK--QSR----QEWEKYNDISVTESSWEEVERDSFGG 216
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1919-2218 |
8.45e-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: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1919 FVGLTNLGATCYLASTIQQLYMIPEARQavFTAKYSEDMKHKTTLLELQKMFTYLMEsecKAYNPRPFcKTY-------- 1990
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRN--FFLLYENYENIKDRKSELVKRLSELIR---KIWNPRNF-KGHvsphellq 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1991 ---TMDKQPLNTGEQKDMTEFFTDLITKV----EEMSPELKNTVKSLFGGVITN-----NVVSLDCEHVSQTAEEFYTVr 2058
Cdd:cd02669 193 avsKVSKKKFSITEQSDPVEFLSWLLNTLhkdlGGSKKPNSSIIHDCFQGKVQIetqkiKPHAEEEGSKDKFFKDSRVK- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2059 cQVADMKNIYESLD-----------------EVTIKDTLEGDNMYTCSHCGKKVraeKRACFKKLPRILSFNTMRYTFNm 2121
Cdd:cd02669 272 -KTSVSPFLLLTLDlpppplfkdgneeniipQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSKN- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2122 vTMMKEKVNTHFSFPLR-LDMTPYTEDflmgksdrkegfkdvgDRSKDTESYEYDLIGVTVHTGT-ADGGHYYSFIRDiv 2199
Cdd:cd02669 347 -NFFKEKNPTIVNFPIKnLDLSDYVHF----------------DKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRH-- 407
|
330
....*....|....*....
gi 568969977 2200 nphaYKNNKWYLFNDAEVK 2218
Cdd:cd02669 408 ----KSTNKWFEIQDLNVK 422
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
2032-2264 |
7.24e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.29 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2032 GGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYES--------LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACF 2103
Cdd:COG5560 634 GQMNFNDAVVISCEWEEKRYLSLFSYDPLWTIREIGAAErtitlqdcLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2104 KKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPL-RLDMTPYTEdflmgksdrkegfkdvgdrSKDTESYEYDLIGVTVH 2182
Cdd:COG5560 714 WRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIdDLDLSGVEY-------------------MVDDPRLIYDLYAVDNH 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2183 TGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSAqlasecfggemttktyDSVTDkfmdfsfekthSAYMLFY 2262
Cdd:COG5560 773 YGGLSGGHYTAYARN------FANNGWYLFDDSRITEVDPE----------------DSVTS-----------SAYVLFY 819
|
..
gi 568969977 2263 KR 2264
Cdd:COG5560 820 RR 821
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2385-2718 |
1.44e-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: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2385 QILIKCPNQIVRQMFQRLCIHVIQRLrpvHAHLYLQPGMEDGSDDMDAsvEDIGGRSCVTRFVRTLLLIMEHgVKPHSKH 2464
Cdd:pfam12030 6 ELLLRNPDAEVRSAFGKLIVFALHKL---KELYGLPDGPCDPDDLEEE--WRSLSDSVLEAVVALLDHLWKE-FHTHLRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2465 LTEYFAFLYEFAKMGEEESQFLLS---LQAISTMVHFYMGTKGPENPQ-VEVLSEEegeeeeeeedilslaeEKYRPAAL 2540
Cdd:pfam12030 80 WDEYFGLLLSYANLGPREVAQLLDlgfLLKCLEIIAADEGDGPPLKYQyARMLRLV----------------EKRRPPSY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2541 EKMIALVALLVEQSRSERHLTLSQT---DMAALTGGKGFPF------LFQH-------------IRDGINIRQTCNLIFS 2598
Cdd:pfam12030 144 EKLIQLLSVLLRCCDLSLPPQSINEgaePLPNSLPDGPFPLtseeadLLRPlgrtngsifvkklLEIDQNPEATRKILRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2599 LCRYNNRLAEHIVSMLFTSIAK-LTPEAANPFFKLLTMLMEFAGGPPgmppfasyilqRIWEVIEYNPSQC--------- 2668
Cdd:pfam12030 224 LLWENPELSDSILKTLLWGIRGaPAHLLRDPFLRAAIVFCEDSWQAH-----------RIHNLIDHVAKQAdslnntegr 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2669 --LDWL--AVQTPRNKL------AHSWVLQNMENWVErFLLAHNYPRVRTSAAYLLVSLI 2718
Cdd:pfam12030 293 afLHFFkrAYQCINCRLgfdkewFASQVLENIPDWAP-PLLSYPDSNVRSETEDFLQEEL 351
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1921-2262 |
1.25e-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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1921 GLTNLGATCYLASTIQQLYMIPearqavftakysedmkhkttllelqkmftYLMEseckaynprpFCKTYTmdkqplntg 2000
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP-----------------------------SLIE----------YLEEFL--------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2001 EQKDMTEFFTDLITKVEemspelkNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEvtiKDTL 2080
Cdd:cd02662 33 EQQDAHELFQVLLETLE-------QLLKFPFDGLLASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTL---EHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2081 EGDNM------YTCSHCgkkvraekRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDmtpytedflmgksd 2154
Cdd:cd02662 103 DDFLSteiiddYKCDRC--------QTVIVRLPQILCIHLSRSVFDG-RGTSTKNSCKVSFPERLP-------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2155 rkegfkdvgdrskdteSYEYDLIGVTVHTGTADGGHYYSFIR-----------DIVNPHAYKN---NKWYLFNDAEVKpf 2220
Cdd:cd02662 160 ----------------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepgSFVRMREGPSstsHPWWRISDTTVK-- 221
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568969977 2221 dsaqlasECfggemttKTYDSVTDKfmdfsfekthSAYMLFY 2262
Cdd:cd02662 222 -------EV-------SESEVLEQK----------SAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1920-2217 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1920 VGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYS----EDMKHKTTLL------------------ELQKMFTYLMESE 1977
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaelASDYPTERRIggrevsrselqrsnqfvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 1978 CKAYNPRPFCKTYTMDKQplNTGEQKDMTEFFTDLITK---VEEMSPELKNT------VKSLFGG--------VITNNVV 2040
Cdd:cd02666 82 TRSVTPSKELAYLALRQQ--DVTECIDNVLFQLEVALEpisNAFAGPDTEDDkeqsdlIKRLFSGktkqqlvpESMGNQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2041 SLDC--EHVSQTA----EEFYTVRCQvADMKNIYESLDEVtikdtLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNT 2114
Cdd:cd02666 160 SVRTktERFLSLLvdvgKKGREIVVL-LEPKDLYDALDRY-----FDYDSLTKLPQRSQVQAQLAQPLQRELISMDRYEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2115 MRYTFNMVTMMKEKVNTHFSfplRLDMTPYTEDFLmgKSDRKEGFKDVgdrskdtESYEYDLIGVTVHTGTADGGHYYSF 2194
Cdd:cd02666 234 PSSIDDIDELIREAIQSESS---LVRQAQNELAEL--KHEIEKQFDDL-------KSYGYRLHAVFIHRGEASSGHYWVY 301
|
330 340
....*....|....*....|...
gi 568969977 2195 IRDivnphaYKNNKWYLFNDAEV 2217
Cdd:cd02666 302 IKD------FEENVWRKYNDETV 318
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2001-2263 |
6.82e-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: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2001 EQKDMTEFFTDLITKVEEMSPELKntvkslfggvitnnvvsLDCEHVSQTAEEfytvrcqvaDMKNIYESLDEVTIKDTl 2080
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEPK-----------------VDIIHGGKKDQD---------DDKLVNERLLQIPVPDD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2081 EGDNMYTCSHCGKkvRAEKRACFKKLPRILSFNTMRYTfnMVTMMKEKVNTHFSFPLRLDMTPYTED----FLMGKSDRK 2156
Cdd:cd02670 75 DDGGGITLEQCLE--QYFNNSVFAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDIPDFVADdpraCSKCQLECR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2157 EGFKDVgDRSKDTESYEYDLIGVTVHTGTA-DGGHYYSFIR-----DIVNPHAYKNNKWYLFndaevkpfDSAQLASECF 2230
Cdd:cd02670 151 VCYDDK-DFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVRygsysLTETDNEAYNAQWVFF--------DDMADRDGVS 221
|
250 260 270
....*....|....*....|....*....|...
gi 568969977 2231 GGemttktyDSVTDKFmdfsfeKTHSAYMLFYK 2263
Cdd:cd02670 222 NG-------FNIPAAR------LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2096-2221 |
9.14e-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: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969977 2096 RAEKRACFKKLPRILSFNTMRYtfNMVTMMKEKVNTHFSFPLRLDMTPYTEDF--LMGKSDRKEGFKDVGDRSKDTES-Y 2172
Cdd:cd02672 134 KAWCDTCCKYQPLEQTTSIRHL--PDILLLVLVINLSVTNGEFDDINVVLPSGkvMQNKVSPKAIDHDKLVKNRGQESiY 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568969977 2173 EYDLIGVTVHTGTAD-GGHYYSFIRDIvnPHAYKNNKWYLFNDAEVKPFD 2221
Cdd:cd02672 212 KYELVGYVCEINDSSrGQHNVVFVIKV--NEESTHGRWYLFNDFLVTPVS 259
|
|
| |
