|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-419 |
0e+00 |
|
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: 511.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFckpfrekvleykaknkrpkETLLSCLADLFYSIATQKKKVGSIAPKKFITRLRKEKEEFD 104
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 105 NYMQQDAHEFLNFLINHINEIILAERNAGPSNGNpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAEILDAERKAEKANRK---------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 185 slnantsvldasgsltatttpiisgnGTGTNGANSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNTSI 264
Cdd:cd02663 96 --------------------------LNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSI 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 265 THCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLFNTSDD 344
Cdd:cd02663 150 TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFNTTDD 229
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649152 345 AVNPDRLYDLTAVVIHCGSGPNRGHYISIVKSHGLWLLFDDDMVDKIEASTIEDFYGltsdIHKSSETGYILFYQ 419
Cdd:cd02663 230 AENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEFFG----DSPNQATAYVLFYQ 300
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
24-418 |
6.92e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 241.19 E-value: 6.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 24 FGLVNFGNTCYSNSVLQALYFCKPFREKVLEY---KAKNKRPKETLLSC-LADLFYSIaTQKKKVGSIAPKKFITRLRKE 99
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplSEDSRYNKDINLLCaLRDLFKAL-QKNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 100 KEEFDNYMQQDAHEFLNFLINHINEIilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngns 179
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHED------------------------------------------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 180 snstgsLNANTSvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVD 259
Cdd:pfam00443 106 ------LNGNHS--------------------------TENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 260 QNTSITH------CLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNrhIKVSHRVVFP 333
Cdd:pfam00443 154 GDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTW--EKLNTEVEFP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 334 LELRLFNTSDDAVNPD----RLYDLTAVVIHCGSgPNRGHYISIVKS--HGLWLLFDDDMVDKIEASTIedfygltsdih 407
Cdd:pfam00443 232 LELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWYKFDDEKVTEVDEETA----------- 299
|
410
....*....|.
gi 24649152 408 KSSETGYILFY 418
Cdd:pfam00443 300 VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
25-419 |
1.60e-60 |
|
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: 197.32 E-value: 1.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFckpfrekvleykaknkrpketllscladlfysiatqkkkvgsiapkkfitrlrkekeefd 104
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 105 nyMQQDAHEFLNFLINHINEIILAERNAGPSNgnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRTSDS------------------------------------------------ 50
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 185 slnantsvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNT-- 262
Cdd:cd02257 51 ---------------------------------SSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGlp 97
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 263 --SITHCLRCFSNTETLCSDNKFKCDnCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRhIKVSHRVVFPLELRLFN 340
Cdd:cd02257 98 qvSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTK-EKLNTKVSFPLELDLSP 175
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 341 ------TSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVK--SHGLWLLFDDDMVDKIEASTIEDFYGLTSdihksseT 412
Cdd:cd02257 176 ylsegeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdpSDGKWYKFNDDKVTEVSEEEVLEFGSLSS-------S 248
|
....*..
gi 24649152 413 GYILFYQ 419
Cdd:cd02257 249 AYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-418 |
2.92e-50 |
|
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: 172.08 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKA-KNKRPKETLLSCLADLFYSIATQKKKvGSIAPKKFITRLRKEKEEF 103
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHsKDCCNEGFCMMCALEAHVERALASSG-PGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 104 DNYMQQDAHEFLNFLINHINEIILAERNAgpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnst 183
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKACLDRFKK--------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 184 gslnantsvLDASGSLTATTTpiisgngtgtnganseptWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNTS 263
Cdd:cd02661 111 ---------LKAVDPSSQETT------------------LVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADS 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 264 ITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFK--YMEQFNRHIKvshrvvFPLELRLFNT 341
Cdd:cd02661 164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSnfRGGKINKQIS------FPETLDLSPY 237
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649152 342 SDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVK-SHGLWLLFDDdmvDKIEASTIEDFYgltsdihksSETGYILFY 418
Cdd:cd02661 238 MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKsSNGKWYNMDD---SKVSPVSIETVL---------SQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
23-423 |
7.67e-48 |
|
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: 166.66 E-value: 7.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSC-LADLFYSIATQKKKVgsIAPKKFITRLRKEKE 101
Cdd:cd02659 2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLaLQRLFLFLQLSESPV--KTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 102 EFDNYMQQDAHEFLNFLINHINEIIlaernagpsngnpKATNQggstsamassiaskssstsnsnsnsnsttnsngnssn 181
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKL-------------KGTGQ------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 182 stgslnantsvldasgsltatttpiisgngtgtngansEPTwVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQN 261
Cdd:cd02659 110 --------------------------------------EGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGK 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 262 TSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLEL----- 336
Cdd:cd02659 151 KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELdmepy 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 337 ------RLFNTSDDAVNPDRLYDLTAVVIHCGSGPNrGHYISIVKS--HGLWLLFDDDMVDKIEASTIED------FYGL 402
Cdd:cd02659 231 tekglaKKEGDSEKKDSESYIYELHGVLVHSGDAHG-GHYYSYIKDrdDGKWYKFNDDVVTPFDPNDAEEecfggeETQK 309
|
410 420
....*....|....*....|....*
gi 24649152 403 TSDI----HKSSETGYILFYQSRDC 423
Cdd:cd02659 310 TYDSgpraFKRTTNAYMLFYERKSP 334
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-418 |
1.85e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 146.75 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLA--------DLFYSIATQkkkvgsiaPKKFITRL 96
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLScamdeifqEFYYSGDRS--------PYGPINLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 97 R---KEKEEFDNYMQQDAHEFLNFLINHINEiiLAERNAGPSNGNpkatnqggstsamassiaskssstsnsnsnsnstt 173
Cdd:cd02660 74 YlswKHSRNLAGYSQQDAHEFFQFLLDQLHT--HYGGDKNEANDE----------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 174 nsngnssnstgslnantsvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFD 253
Cdd:cd02660 117 --------------------------------------------SHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 254 LQVDVDQNT---------------SITHCLRCFSNTETLCSDNkFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYmE 318
Cdd:cd02660 153 LSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEH-S 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 319 QFNRHIKVSHRVVFPLELRL---------FNTSDDAVNPDRLYDLTAVVIHCGSgPNRGHYISIVKSH-GLWLLFDDDMV 388
Cdd:cd02660 231 LNKTSRKIDTYVQFPLELNMtpytsssigDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQGdGQWFKFDDAMI 309
|
410 420 430
....*....|....*....|....*....|
gi 24649152 389 DKIeasTIEDFYGltsdihkssETGYILFY 418
Cdd:cd02660 310 TRV---SEEEVLK---------SQAYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-419 |
2.35e-39 |
|
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: 140.89 E-value: 2.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 228 FQGILTSETRCLNCETVSSKDENFFDLQVDVDQNT------SITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVK 301
Cdd:cd02674 44 FQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTIS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 302 KLPMILALHLKRFKYmeQFNRHIKVSHRVVFPLE---LRLFNTSDDAVNPDRlYDLTAVVIHCGSGpNRGHYISIVKS-- 376
Cdd:cd02674 124 RLPKVLIIHLKRFSF--SRGSTRKLTTPVTFPLNdldLTPYVDTRSFTGPFK-YDLYAVVNHYGSL-NGGHYTAYCKNne 199
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24649152 377 HGLWLLFDDDMVDKIEASTIEdfygltsdihksSETGYILFYQ 419
Cdd:cd02674 200 TNDWYKFDDSRVTKVSESSVV------------SSSAYILFYE 230
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-418 |
7.30e-38 |
|
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: 140.03 E-value: 7.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLA--DLFYSIAtqkkkvGSIAPKKFITRLRKEKEE 102
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDEL------ANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 103 FDNYMQQDAHEFLNFLINHINEIilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssns 182
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQEL--------------------------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 183 tgslnantsvldasgsltatttpiisgngtgtnganseptwVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDV---- 258
Cdd:cd02671 123 -----------------------------------------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVqese 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 259 ----DQNTSITHCLRC-----------FSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRF----KYMEQ 319
Cdd:cd02671 162 lsksEESSEISPDPKTemktlkwaisqFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFaangSEFDC 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 320 FNRHIKVSHRVVFPLELRLFNTSDDAVNPDrlYDLTAVVIHCGSGPNRGHYISIVKshglWLLFDDdmvDKIEASTIEDF 399
Cdd:cd02671 242 YGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAYVR----WLLFDD---SEVKVTEEKDF 312
|
410
....*....|....*....
gi 24649152 400 YGLTSDIHKSSETGYILFY 418
Cdd:cd02671 313 LEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-418 |
6.09e-37 |
|
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: 137.17 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEY-----------KAKNKRPKETLLSCLADLFYSIATQKKKVgsIAPKKFI 93
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECnstedaelknmPPDKPHEPQTIIDQLQLIFAQLQFGNRSV--VDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 94 TRLRkekeeFDNYMQQDAHEFLNFLINHINEIILaernagpSNGNPKATNqggstsamassiaskssstsnsnsnsnstt 173
Cdd:cd02668 79 KALG-----LDTGQQQDAQEFSKLFLSLLEAKLS-------KSKNPDLKN------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 174 nsngnssnstgslnantsvldasgsltatttpiisgngtgtnganseptWVHEIFQGILTSETRCLNCETVSSKDENFFD 253
Cdd:cd02668 117 -------------------------------------------------IVQDLFRGEYSYVTQCSKCGRESSLPSKFYE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 254 LQVDVDQNTSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFP 333
Cdd:cd02668 148 LELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 334 LELRLFNTSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVK--SHGLWLLFDDDMVDKIEASTIEDfyGLTSDIHK--- 408
Cdd:cd02668 228 EILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdeQTGEWYKFNDEDVEEMPGKPLKL--GNSEDPAKprk 305
|
410
....*....|....*...
gi 24649152 409 --------SSETGYILFY 418
Cdd:cd02668 306 seikkgthSSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-419 |
7.75e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 134.16 E-value: 7.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKKVGSiAPKKFITRLRKEKeeFD 104
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA-PPDYFLEASRPPW--FT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 105 NYMQQDAHEFLNFLINHINeiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02664 78 PGSQQDCSEYLRYLLDRLH------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 185 slnantsvldasgsltatttpiisgngtgtngansepTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVdqnTSI 264
Cdd:cd02664 97 -------------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSV 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 265 THCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRL------ 338
Cdd:cd02664 137 QDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLpvrves 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 339 -------------FNTSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVKS----------------------HGLWLLF 383
Cdd:cd02664 217 kssesplekkeeeSGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLF 296
|
410 420 430
....*....|....*....|....*....|....*.
gi 24649152 384 DDDMVDKIEASTIEDFYGLtsdihKSSETGYILFYQ 419
Cdd:cd02664 297 NDSRVTFSSFESVQNVTSR-----FPKDTPYILFYE 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-419 |
3.64e-32 |
|
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: 123.27 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEykaknkRPKEtLLSCLadlfysiatqkkkvgsiapkkfitrlRKEKEEFD 104
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------TPKE-LFSQV--------------------------CRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 105 NYMQQDAHEFLNFLINHINeiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR------------------------------------------------------------- 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 185 slnantsvldasgsltatttpiisgngtgtngansepTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQ----VDVDQ 260
Cdd:cd02667 67 -------------------------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKS 109
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 261 NTSITHCLRCFSNTETLCSDNKFKCDNCCsyqEAQKRMRVKKLPMILALHLKRFKyMEQFNRHIKVSHRVVFP--LELRL 338
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ-QPRSANLRKVSRHVSFPeiLDLAP 185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 339 FNTSDDAVNPDR---LYDLTAVVIHCGSGpNRGHYISIVKSHGLWLLFDDDMVDKIEASTIED-----FYGLTSDIHKSS 410
Cdd:cd02667 186 FCDPKCNSSEDKssvLYRLYGVVEHSGTM-RSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPgsgqwYYISDSDVREVS 264
|
410
....*....|....*
gi 24649152 411 ET------GYILFYQ 419
Cdd:cd02667 265 LEevlkseAYLLFYE 279
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-418 |
8.16e-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 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: 112.04 E-value: 8.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKET---LLSCLADLFysiATQKKKVGSIAPKKFITRLRK--- 98
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSsdnLTNALRDLF---DTMDKKQEPVPPIEFLQLLRMafp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 99 ---EKEEFDNYMQQDAHEFLNFLinhineiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttns 175
Cdd:cd02657 78 qfaEKQNQGGYAQQDAEECWSQL--------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 176 ngnssnstgsLNANTSVLDasgsltatttpiisgngtgtnGANSEPTWVHEIFQGILTSETRCLNCETV-SSKDENFFDL 254
Cdd:cd02657 101 ----------LSVLSQKLP---------------------GAGSKGSFIDQLFGIELETKMKCTESPDEeEVSTESEYKL 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 255 QVDVDQNTSITH----CLRCFSNTETLCSDnkfKCDNCCSYQeaqKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRV 330
Cdd:cd02657 150 QCHISITTEVNYlqdgLKKGLEEEIEKHSP---TLGRDAIYT---KTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKV 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 331 VFPLELRLFntsdDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVKS--HGLWLLFDDDMVDKIEASTIEDFYGlTSDIHk 408
Cdd:cd02657 224 KFPFELDLY----ELCTPSGYYELVAVITHQGRSADSGHYVAWVRRknDGKWIKFDDDKVSEVTEEDILKLSG-GGDWH- 297
|
410
....*....|
gi 24649152 409 sseTGYILFY 418
Cdd:cd02657 298 ---IAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
23-401 |
9.49e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 110.35 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKKVGSiapkkfiTRLRKEK-- 100
Cdd:COG5077 193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDT-------TELTRSFgw 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 101 EEFDNYMQQDAHEFLNFLINHIneiilaERNAgpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnss 180
Cdd:COG5077 266 DSDDSFMQHDIQEFNRVLQDNL------EKSM------------------------------------------------ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 181 nstgslnANTSVLDAsgsltatttpiisgngtgtnganseptwVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQ 260
Cdd:COG5077 292 -------RGTVVENA----------------------------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 261 NTSITHCLRCFSNTETLCSDNKFKCDNCcSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLF- 339
Cdd:COG5077 337 MKNLQESFRRYIQVETLDGDNRYNAEKH-GLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLp 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649152 340 ---NTSDDAVNPDRLYDLTAVVIHCGSGPNrGHYISIVKSH--GLWLLFDDDMVDKI-EASTIEDFYG 401
Cdd:COG5077 416 fldRDADKSENSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFDDTRVTRAtEKEVLEENFG 482
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-419 |
9.19e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 97.78 E-value: 9.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPK-------ETLLSCLADLF----YSIATQKKKVGS-----IA 88
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVvdpandlNCQLIKLADGLlsgrYSKPASLKSENDpyqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 89 PKKFITRLRKEKEEFDNYMQQDAHEFLNFLINHIneiilaERNAGPSNGnpkatnqggstsamassiaskssstsnsnsn 168
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKL------DRESFKNLG------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 169 snsttnsngnssnstgslnantsvldasgsltatttpiisgngtgtnganSEPTwvhEIFQGILTSETRCLNCETVSSKD 248
Cdd:cd02658 124 --------------------------------------------------LNPN---DLFKFMIEDRLECLSCKKVKYTS 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 249 ENFFDLQVDVD--------------QNTSITHCLRCFSNTETLcsdnKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRF 314
Cdd:cd02658 151 ELSEILSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 315 KYMEQFnRHIKVSHRVVFPLELRlfntsddavnPDRlYDLTAVVIHCGSGPNRGHYISIVK----SHGLWLLFDDdmvDK 390
Cdd:cd02658 227 QLLENW-VPKKLDVPIDVPEELG----------PGK-YELIAFISHKGTSVHSGHYVAHIKkeidGEGKWVLFND---EK 291
|
410 420
....*....|....*....|....*....
gi 24649152 391 IEASTIEDFygltsdiHKssETGYILFYQ 419
Cdd:cd02658 292 VVASQDPPE-------MK--KLGYIYFYQ 311
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
263-421 |
2.41e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 87.63 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 263 SIT--HCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRhiKVSHRVVFP---LELR 337
Cdd:COG5560 674 TITlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYPiddLDLS 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 338 LFNTSDDavNPDRLYDLTAVVIHCGsGPNRGHYISIVK--SHGLWLLFDDDMVDKIEAstiedfygltSDIHKSSetGYI 415
Cdd:COG5560 752 GVEYMVD--DPRLIYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRITEVDP----------EDSVTSS--AYV 816
|
....*.
gi 24649152 416 LFYQSR 421
Cdd:COG5560 817 LFYRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
25-418 |
4.01e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 81.00 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPfreKVLEYKAKNKRPKETLLSCLADLFySIATQKKKVgsiapkKFITRLRKEKE--- 101
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLP---KLDELLDDLSKELKVLKNVIRKPE-PDLNQEEAL------KLFTALWSSKEhkv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 102 --EFDNYMQQDAHEFLNFLINHINeiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngns 179
Cdd:COG5533 71 gwIPPMGSQEDAHELLGKLLDELK-------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 180 snstgslnantsvLDASGSLTATTTPIisgngTGTNGANSEPTWvHEIFqgILTSETRCLNCETVSSKDENFFDLQVDvd 259
Cdd:COG5533 95 -------------LDLVNSFTIRIFKT-----TKDKKKTSTGDW-FDII--IELPDQTWVNNLKTLQEFIDNMEELVD-- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 260 qntsithclrcfSNTETLCSDNKFKcdnccsyqEAQKRMR----VKKLPMILALHLKRFKYMeqfNRHIKVSHRVVFPLE 335
Cdd:COG5533 152 ------------DETGVKAKENEEL--------EVQAKQEyevsFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFE 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 336 LRLFNTSDDAVNPDRLYDLTAVVIHCGSgPNRGHYISIVKSHGLWLLFDDDMVDKIEASTIEDfygltsdihKSSETGYI 415
Cdd:COG5533 209 LPVKHDQILNIVKETYYDLVGFVLHQGS-LEGGHYIAYVKKGGKWEKANDSDVTPVSEEEAIN---------EKAKNAYL 278
|
...
gi 24649152 416 LFY 418
Cdd:COG5533 279 YFY 281
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
218-385 |
2.42e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 79.24 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 218 NSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDV----------DQNTSITHCLRCFSNTETLcsdNKFKCDN 287
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYprkpssnnkkPPNQTFSSILKSSLERETT---TKAWCEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 288 CCSYQEAQKRMRVKKLPMILALHLKRFKymEQFNRHIKVshRVVFPLELRLFNTSDDAVNPD-RLYDLTAVVIHCGSGPN 366
Cdd:pfam13423 199 CKRYQPLESRRTVRNLPPVLSLNAALTN--EEWRQLWKT--PGWLPPEIGLTLSDDLQGDNEiVKYELRGVVVHIGDSGT 274
|
170 180
....*....|....*....|....*...
gi 24649152 367 RGHYISIVK---------SHGLWLLFDD 385
Cdd:pfam13423 275 SGHLVSFVKvadseledpTESQWYLFND 302
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-419 |
9.94e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 76.25 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 228 FQGILTSETRCLNCETVSSKDENFFD---LQV---DVDQNTSITHCLRCFSNTETlCSDnkFKCDNCcsyQEAqkrmrVK 301
Cdd:cd02662 56 FDGLLASRIVCLQCGESSKVRYESFTmlsLPVpnqSSGSGTTLEHCLDDFLSTEI-IDD--YKCDRC---QTV-----IV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 302 KLPMILALHLKRFkymeQFNRHI---KVSHRVVFPLELrlfntsddavnPDRLYDLTAVVIHCGSgPNRGHYISIVKSHG 378
Cdd:cd02662 125 RLPQILCIHLSRS----VFDGRGtstKNSCKVSFPERL-----------PKVLYRLRAVVVHYGS-HSSGHYVCYRRKPL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24649152 379 LWLLFDDDMVD---KIEASTIEDFYGL---------TSDIHKSSETgYILFYQ 419
Cdd:cd02662 189 FSKDKEPGSFVrmrEGPSSTSHPWWRIsdttvkevsESEVLEQKSA-YMLFYE 240
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
26-418 |
1.33e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 64.09 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 26 LVNFGNTCYSNSVLQALyfckpfrekvleykaknkrpketllscladlfysiatqkkkvgsiapkkfiTRLRKEKEEFDN 105
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL---------------------------------------------------SSIGKINTEFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 106 YMQQDAHEFLNFLINHINEIILAER-NAGPSNGNPKATNqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02673 31 DDQQDAHEFLLTLLEAIDDIMQVNRtNVPPSNIEIKRLN----------------------------------------- 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 185 slnantsvldasgsltatttPIisgngtgtnganseptwvhEIFQGILTSETRCLNC--ETVSSKDENFFDLQV---DVD 259
Cdd:cd02673 70 --------------------PL-------------------EAFKYTIESSYVCIGCsfEENVSDVGNFLDVSMidnKLD 110
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 260 QNTSITHCLRCFSNTETLCSDnkfkcdncCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLF 339
Cdd:cd02673 111 IDELLISNFKTWSPIEKDCSS--------CKCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEIMKKYCGTDA 182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 340 NtsddavnpdrlYDLTAVVIHCGSGPNRGHYISIVKS---HGLWLLFDDDMVDKIEASTIedfygltsdIHKSSETGYIL 416
Cdd:cd02673 183 K-----------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEIRPVSKNDV---------STNARSSGYLI 242
|
..
gi 24649152 417 FY 418
Cdd:cd02673 243 FY 244
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
23-392 |
2.38e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 52.71 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYK--AKNKRPKETLLSCLADLFYSIATQKKKVGSIAPKKF---ITRLR 97
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnyENIKDRKSELVKRLSELIRKIWNPRNFKGHVSPHELlqaVSKVS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 98 KEKeeFDNYMQQDAHEFLNFLINHINeiilaernagpsngnpKATNQGGSTsamassiaskssstsnsnsnsnsttnsng 177
Cdd:cd02669 199 KKK--FSITEQSDPVEFLSWLLNTLH----------------KDLGGSKKP----------------------------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 178 nssnstgslnaNTSVLDAS--GSLTATTTPIISGNGTGTNGANseptwVHEIFQGILTSETRCLncetVSSKDENFFDLQ 255
Cdd:cd02669 232 -----------NSSIIHDCfqGKVQIETQKIKPHAEEEGSKDK-----FFKDSRVKKTSVSPFL----LLTLDLPPPPLF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 256 VDVDQNTSITHclrcFSNTETLcsdNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRF-KYMEQFNRHIKVshrVVFPL 334
Cdd:cd02669 292 KDGNEENIIPQ----VPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFsKNNFFKEKNPTI---VNFPI 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649152 335 ELRLF----NTSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIV--KSHGLWLLFDDDMVDKIE 392
Cdd:cd02669 362 KNLDLsdyvHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrhKSTNKWFEIQDLNVKEVL 425
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
25-59 |
1.80e-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: 49.41 E-value: 1.80e-06
10 20 30
....*....|....*....|....*....|....*
gi 24649152 25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKN 59
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESK 37
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
224-419 |
9.76e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 46.74 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 224 VHEIFQGIL--TSETRCLN----CETVSSKDENFFDLQVDVD--QNTSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQ 295
Cdd:cd02672 68 LIQNFTRFLleTISQDQLGtpfsCGTSRNSVSLLYTLSLPLGstKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 296 KRMRVKKLPMI----LALHLKRFKYMEQFNRHIKVS-----HRVVFPLELRLFNTSDDAVNPDRLYDLTAVVIHCGSGPN 366
Cdd:cd02672 148 QTTSIRHLPDIlllvLVINLSVTNGEFDDINVVLPSgkvmqNKVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSR 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24649152 367 RGHYISIV------KSHGLWLLFDDDMVDKIeastiedfygltsdihksSETGYILFYQ 419
Cdd:cd02672 228 GQHNVVFVikvneeSTHGRWYLFNDFLVTPV------------------SELAYILLYQ 268
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
301-419 |
1.15e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 43.28 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649152 301 KKLPMILALHLKRFKYMEQFNrhIKVSHRVVFPLELRL----------------------FNTSDDAVNPDRLYDLTAVV 358
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKA--QKMFKKILIPDEIDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAV 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24649152 359 IHCGSGPNRGHYISIVK--SHGL-----------WLLFdDDMVDKIEAstiedFYGLTSDIHKSSETGYILFYQ 419
Cdd:cd02670 174 CHRGTSLETGHYVAFVRygSYSLtetdneaynaqWVFF-DDMADRDGV-----SNGFNIPAARLLEDPYMLFYQ 241
|
|
| |
