NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24756890|gb|AAN64154|]
View 

Putative ubiquitin-specific protease 3 [Oryza sativa Japonica Group]

Protein Classification

Peptidase_C19G domain-containing protein (domain architecture ID 10119250)

Peptidase_C19G domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 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: 504.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFcvpfreqlleyyannkstgdveDNMLTCLADLFSQISNQKKKTGVIAPKRFIQRLKKQNE 103
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF----------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENE 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 IFRSYMHQDAHEFLNFLLNELVDILEKESKVVAEPcensslkknsngpiNVQLNGTKKEPVPTLVHKCFQGILTNETRCL 183
Cdd:cd02663  59 LFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKAN--------------RKLNNNNNAEPQPTWVHEIFQGILTNETRCL 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKYIEQ 263
Cdd:cd02663 125 TCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQ 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 264 LGRYKKLSYRVVFPLELKLINTVD---NSDLEYSLFAVLVHVGSGPNHGHYISLVKSHNHWLFFDDENVEMTDESMVQTF 340
Cdd:cd02663 205 LNRYIKLFYRVVFPLELRLFNTTDdaeNPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEF 284
                       330       340
                ....*....|....*....|
gi 24756890 341 FGsaqeFSGNTDNGYILFYE 360
Cdd:cd02663 285 FG----DSPNQATAYVLFYQ 300
 
Name Accession Description Interval E-value
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 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: 504.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFcvpfreqlleyyannkstgdveDNMLTCLADLFSQISNQKKKTGVIAPKRFIQRLKKQNE 103
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF----------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENE 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 IFRSYMHQDAHEFLNFLLNELVDILEKESKVVAEPcensslkknsngpiNVQLNGTKKEPVPTLVHKCFQGILTNETRCL 183
Cdd:cd02663  59 LFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKAN--------------RKLNNNNNAEPQPTWVHEIFQGILTNETRCL 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKYIEQ 263
Cdd:cd02663 125 TCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQ 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 264 LGRYKKLSYRVVFPLELKLINTVD---NSDLEYSLFAVLVHVGSGPNHGHYISLVKSHNHWLFFDDENVEMTDESMVQTF 340
Cdd:cd02663 205 LNRYIKLFYRVVFPLELRLFNTTDdaeNPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEF 284
                       330       340
                ....*....|....*....|
gi 24756890 341 FGsaqeFSGNTDNGYILFYE 360
Cdd:cd02663 285 FG----DSPNQATAYVLFYQ 300
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
23-359 2.65e-91

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 275.81  E-value: 2.65e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890    23 FGLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNK-STGDVEDNMLTCLADLFSQISNQKKKTGvIAPKRFIQRLKKQ 101
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRISPLSEdSRYNKDINLLCALADLFKALQSEKKSSS-VSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   102 NEIFRSYMHQDAHEFLNFLLNELVDILekeskvvaepcensslkknsngpinvqlNGTKKEPVPTLVHKCFQGILTNETR 181
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDL----------------------------NGKHSTENESLITDLFRGQLKSRLK 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   182 CLRCETVTDRDETFFDLSLDIEQNSS--ITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:pfam00443 132 CLNCGKESYTFEPFLDLSLPIPSLKNydLQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFS 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   260 YieQLGRYKKLSYRVVFPLELKLINTVDNSDLE-------YSLFAVLVHVGSgPNHGHYISLVKSH--NHWLFFDDENVE 330
Cdd:pfam00443 212 Y--NRSTWEKLNTEVEFPEELDLSEYLAEGLDEkeveptkYRLVAVVVHSGS-LSSGHYIAYIKKYenGRWYKFDDEKVT 288
                         330       340
                  ....*....|....*....|....*....
gi 24756890   331 MTDESMVQtffgsaqefsgnTDNGYILFY 359
Cdd:pfam00443 289 EVDEEEVL------------NKSAYILFY 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
24-360 9.77e-42

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 150.56  E-value: 9.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLE-YYANNKSTGDVEDNMLTCLADLFSQISNQKKKTG--VIAPKRFIQRLKK 100
Cdd:COG5533  73 GLRNKGNTCYMNCALQCLLSIGDLNTMLQGrFYLQNINTDFPRGKPGSNAFKQFIALYETPGCHGpkSISPRNFIDILSG 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 101 QNEIFRSYMHQDAHEFLNFLLNEL-VDILEKESKVVAEPC--------ENSSLKKNSNGPINVQLNGTKkepvpTLVHKC 171
Cdd:COG5533 153 RNKLFSGDMQQDSQEFLIFFLDLLhEDLNGNKSRSPILELkdefeevrEELPLSHFSHHEWNLHLRSNK-----SLVAKT 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 172 FQGILTNETRCLRCETVTDRDETFFDLSLDIEQNSS--ITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPN 249
Cdd:COG5533 228 FFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYEVVQlgLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRKRMEILVLPD 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 250 ILVIHLKRFKyIEQLGRYK---KLSYRVVFPLEL---KLINT-VDNSDLEYSLFAVLVHVGSgPNHGHYISLVKSHNHWL 322
Cdd:COG5533 308 VLIIHISRFH-ISVMGRKKidtPQGWKNTASVEVnvtLLFNNgIGYIPRKYSLLGVVCHNGT-LNGGHYFSEVKRSGTWN 385
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 24756890 323 FFDDenvemtdeSMVQTFFGSaqeFSGNTDNGYILFYE 360
Cdd:COG5533 386 VYDD--------SQVRKGSRT---TSGSHPSSYILFYT 412
 
Name Accession Description Interval E-value
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 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: 504.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFcvpfreqlleyyannkstgdveDNMLTCLADLFSQISNQKKKTGVIAPKRFIQRLKKQNE 103
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF----------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENE 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 IFRSYMHQDAHEFLNFLLNELVDILEKESKVVAEPcensslkknsngpiNVQLNGTKKEPVPTLVHKCFQGILTNETRCL 183
Cdd:cd02663  59 LFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKAN--------------RKLNNNNNAEPQPTWVHEIFQGILTNETRCL 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKYIEQ 263
Cdd:cd02663 125 TCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQ 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 264 LGRYKKLSYRVVFPLELKLINTVD---NSDLEYSLFAVLVHVGSGPNHGHYISLVKSHNHWLFFDDENVEMTDESMVQTF 340
Cdd:cd02663 205 LNRYIKLFYRVVFPLELRLFNTTDdaeNPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEF 284
                       330       340
                ....*....|....*....|
gi 24756890 341 FGsaqeFSGNTDNGYILFYE 360
Cdd:cd02663 285 FG----DSPNQATAYVLFYQ 300
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
23-359 2.65e-91

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 275.81  E-value: 2.65e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890    23 FGLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNK-STGDVEDNMLTCLADLFSQISNQKKKTGvIAPKRFIQRLKKQ 101
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRISPLSEdSRYNKDINLLCALADLFKALQSEKKSSS-VSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   102 NEIFRSYMHQDAHEFLNFLLNELVDILekeskvvaepcensslkknsngpinvqlNGTKKEPVPTLVHKCFQGILTNETR 181
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDL----------------------------NGKHSTENESLITDLFRGQLKSRLK 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   182 CLRCETVTDRDETFFDLSLDIEQNSS--ITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:pfam00443 132 CLNCGKESYTFEPFLDLSLPIPSLKNydLQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFS 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   260 YieQLGRYKKLSYRVVFPLELKLINTVDNSDLE-------YSLFAVLVHVGSgPNHGHYISLVKSH--NHWLFFDDENVE 330
Cdd:pfam00443 212 Y--NRSTWEKLNTEVEFPEELDLSEYLAEGLDEkeveptkYRLVAVVVHSGS-LSSGHYIAYIKKYenGRWYKFDDEKVT 288
                         330       340
                  ....*....|....*....|....*....
gi 24756890   331 MTDESMVQtffgsaqefsgnTDNGYILFY 359
Cdd:pfam00443 289 EVDEEEVL------------NKSAYILFY 305
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
24-360 1.40e-67

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: 213.50  E-value: 1.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFcvpfreqlleyyannkstgdvednmltcladlfsqisnqkkktgviapkrfiqrlkkqne 103
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 ifrsyMHQDAHEFLNFLLNELVDILEKESKvvaepcensslkknsngpinvqlNGTKKEPVPTLVHKCFQGILTNETRCL 183
Cdd:cd02257  21 -----EQQDAHEFLLFLLDKLHEELKKSSK-----------------------RTSDSSSLKSLIHDLFGGKLESTIVCL 72
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDI----EQNSSITSCLKNFSSTETLNAEDKFFCDKCcSLQEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:cd02257  73 ECGHESVSTEPELFLSLPLpvkgLPQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFS 151
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 260 YIEQlGRYKKLSYRVVFPLELKL---------INTVDNSDLEYSLFAVLVHVGSGPNHGHYISLVKSHNH--WLFFDDEN 328
Cdd:cd02257 152 FNED-GTKEKLNTKVSFPLELDLspylsegekDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDgkWYKFNDDK 230
                       330       340       350
                ....*....|....*....|....*....|..
gi 24756890 329 VEMTDESMVqtffgsaQEFSGNTDNGYILFYE 360
Cdd:cd02257 231 VTEVSEEEV-------LEFGSLSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-359 7.75e-63

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: 202.89  E-value: 7.75e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYyANNKSTGDVEDNMLTCLADLFSQISNQKKKTgvIAPKRFIQRLKKQNE 103
Cdd:cd02661   3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSR-EHSKDCCNEGFCMMCALEAHVERALASSGPG--SAPRIFSSNLKQISK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 IFRSYMHQDAHEFLNFLLnelvdilekeskvvaEPCENSSLKKNSNGPINVQLNGTKkepvpTLVHKCFQGILTNETRCL 183
Cdd:cd02661  80 HFRIGRQEDAHEFLRYLL---------------DAMQKACLDRFKKLKAVDPSSQET-----TLVQQIFGGYLRSQVKCL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKYIeq 263
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF-- 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 264 lgRYKKLSYRVVFPLELKLINTVDNSD---LEYSLFAVLVHVGSGPNHGHYISLVK-SHNHWLFFDDENVEMTDESMVQt 339
Cdd:cd02661 218 --RGGKINKQISFPETLDLSPYMSQPNdgpLKYKLYAVLVHSGFSPHSGHYYCYVKsSNGKWYNMDDSKVSPVSIETVL- 294
                       330       340
                ....*....|....*....|
gi 24756890 340 ffgsaqefsgnTDNGYILFY 359
Cdd:cd02661 295 -----------SQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
21-360 5.93e-58

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: 190.93  E-value: 5.93e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  21 RYFGLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNKSTGDVEDNMLTCLADLFSQISNQKKKTGVIAPKRFiqrlKK 100
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTR----SF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 101 QNEIFRSYMHQDAHEFLNFLLNELvdilekeskvvaepcENSSlkknsngpinvqlngtKKEPVPTLVHKCFQGILTNET 180
Cdd:cd02659  77 GWDSLNTFEQHDVQEFFRVLFDKL---------------EEKL----------------KGTGQEGLIKNLFGGKLVNYI 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 181 RCLRCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKY 260
Cdd:cd02659 126 ICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEF 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 261 IEQLGRYKKLSYRVVFPLELKL--------------INTVDNSDLEYSLFAVLVHvgSGPNH-GHYISLVKS--HNHWLF 323
Cdd:cd02659 206 DFETMMRIKINDRFEFPLELDMepytekglakkegdSEKKDSESYIYELHGVLVH--SGDAHgGHYYSYIKDrdDGKWYK 283
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 24756890 324 FDDENVEMTDESMV-QTFFGSAQEFSGN---------TDNGYILFYE 360
Cdd:cd02659 284 FNDDVVTPFDPNDAeEECFGGEETQKTYdsgprafkrTTNAYMLFYE 330
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-359 8.50e-49

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: 167.16  E-value: 8.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNKSTGDVEDNMLTC-LADLFSQISNQKKKTGVIaPKRFIQRLKKQN 102
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCaMDEIFQEFYYSGDRSPYG-PINLLYLSWKHS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 103 EIFRSYMHQDAHEFLNFLLNELvdilEKESKVVAEPCENSSlkknsngpinvqlngtkkePVPTLVHKCFQGILTNETRC 182
Cdd:cd02660  81 RNLAGYSQQDAHEFFQFLLDQL----HTHYGGDKNEANDES-------------------HCNCIIHQTFSGSLQSSVTC 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 183 LRCETVTDRDETFFDLSLDIEQNS---------------SITSCLKNFSSTETLnAEDKFFCDKCCSLQEAQKRMKIKKP 247
Cdd:cd02660 138 QRCGGVSTTVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 248 PNILVIHLKRFKYiEQLGRYKKLSYRVVFPLEL------------KLINTVDNSDLEYSLFAVLVHVGSgPNHGHYISLV 315
Cdd:cd02660 217 PPVLCFQLKRFEH-SLNKTSRKIDTYVQFPLELnmtpytsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYC 294
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 24756890 316 KSHN-HWLFFDDENVEMTDESMVQtffgsaqefsgnTDNGYILFY 359
Cdd:cd02660 295 RQGDgQWFKFDDAMITRVSEEEVL------------KSQAYLLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 2.32e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 162.84  E-value: 2.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALyfcvpfreqlleyyannkstgdvednmltcladlfsqisnqkkktgviapkrfiqrlkkqne 103
Cdd:cd02674   1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 ifrSYMHQDAHEFLNFLLNELvdilekESKVVAEpcensslkknsngpinvqlngtkkepvptlvhkcFQGILTNETRCL 183
Cdd:cd02674  19 ---SADQQDAQEFLLFLLDGL------HSIIVDL----------------------------------FQGQLKSRLTCL 55
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDIEQNS------SITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKR 257
Cdd:cd02674  56 TCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 258 FKYieQLGRYKKLSYRVVFPLEL-----KLINTVDNSDLEYSLFAVLVHVGSGpNHGHYISLVKS--HNHWLFFDDENVE 330
Cdd:cd02674 136 FSF--SRGSTRKLTTPVTFPLNDldltpYVDTRSFTGPFKYDLYAVVNHYGSL-NGGHYTAYCKNneTNDWYKFDDSRVT 212
                       330       340       350
                ....*....|....*....|....*....|
gi 24756890 331 MTDESmvqtffgsaqefSGNTDNGYILFYE 360
Cdd:cd02674 213 KVSES------------SVVSSSAYILFYE 230
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-330 1.17e-46

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: 161.43  E-value: 1.17e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLL--------EYYANNKSTGDVEDNMLTCLADLFSQISNQKKKtgVIAPKRFI 95
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstedaELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRS--VVDPSGFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  96 QRLKKQNEifrsyMHQDAHEFLNFLLNELVDILEKESkvvaepceNSSLKknsngpinvqlngtkkepvpTLVHKCFQGI 175
Cdd:cd02668  79 KALGLDTG-----QQQDAQEFSKLFLSLLEAKLSKSK--------NPDLK--------------------NIVQDLFRGE 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 176 LTNETRCLRCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHL 255
Cdd:cd02668 126 YSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 256 KRFKYIEQLGRYKKLSYRVVFPLELKLINTVDNSDL---EYSLFAVLVHVGSGPNHGHYISLVKSHNH--WLFFDDENVE 330
Cdd:cd02668 206 LRFVFDRKTGAKKKLNASISFPEILDMGEYLAESDEgsyVYELSGVLIHQGVSAYSGHYIAHIKDEQTgeWYKFNDEDVE 285
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-359 1.53e-45

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: 158.52  E-value: 1.53e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNKStgdVEDNMLTCLadlfsqiSNQKKKTGVIA---PKRFIQRLKK 100
Cdd:cd02671  26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISS---VEQLQSSFL-------LNPEKYNDELAnqaPRRLLNALRE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 101 QNEIFRSYMHQDAHEFLNFLLNELVDILEKEskvvaepcensslkknsngpinvqlngtkkepvptlvhkcFQGILTNET 180
Cdd:cd02671  96 VNPMYEGYLQHDAQEVLQCILGNIQELVEKD----------------------------------------FQGQLVLRT 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 181 RCLRCETVTDRDETFFDLSLDI--------EQNSSITSCLK-----------NFSSTETLNAEDKFFCDKCCSLQEAQKR 241
Cdd:cd02671 136 RCLECETFTERREDFQDISVPVqeselsksEESSEISPDPKtemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERS 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 242 MKIKKPPNILVIHLKRF----KYIEQLGRYKKLSYRVVFPLELKLINTVDNSDLE-YSLFAVLVHVGSGPNHGHYISLVK 316
Cdd:cd02671 216 LLFDKLPEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDvYRLFAVVMHSGATISSGHYTAYVR 295
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 24756890 317 shnhWLFFDDENVEMTDEsmvQTFFGSAQEFSGNTDNGYILFY 359
Cdd:cd02671 296 ----WLLFDDSEVKVTEE---KDFLEALSPNTSSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
24-360 9.77e-42

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 150.56  E-value: 9.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLE-YYANNKSTGDVEDNMLTCLADLFSQISNQKKKTG--VIAPKRFIQRLKK 100
Cdd:COG5533  73 GLRNKGNTCYMNCALQCLLSIGDLNTMLQGrFYLQNINTDFPRGKPGSNAFKQFIALYETPGCHGpkSISPRNFIDILSG 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 101 QNEIFRSYMHQDAHEFLNFLLNEL-VDILEKESKVVAEPC--------ENSSLKKNSNGPINVQLNGTKkepvpTLVHKC 171
Cdd:COG5533 153 RNKLFSGDMQQDSQEFLIFFLDLLhEDLNGNKSRSPILELkdefeevrEELPLSHFSHHEWNLHLRSNK-----SLVAKT 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 172 FQGILTNETRCLRCETVTDRDETFFDLSLDIEQNSS--ITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPN 249
Cdd:COG5533 228 FFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYEVVQlgLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRKRMEILVLPD 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 250 ILVIHLKRFKyIEQLGRYK---KLSYRVVFPLEL---KLINT-VDNSDLEYSLFAVLVHVGSgPNHGHYISLVKSHNHWL 322
Cdd:COG5533 308 VLIIHISRFH-ISVMGRKKidtPQGWKNTASVEVnvtLLFNNgIGYIPRKYSLLGVVCHNGT-LNGGHYFSEVKRSGTWN 385
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 24756890 323 FFDDenvemtdeSMVQTFFGSaqeFSGNTDNGYILFYE 360
Cdd:COG5533 386 VYDD--------SQVRKGSRT---TSGSHPSSYILFYT 412
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 1.13e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 144.45  E-value: 1.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYyannkstgdvednmltcLADLFSQISNQkkktgviAPKrfiqrlkkqne 103
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-----------------PKELFSQVCRK-------APQ----------- 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 iFRSYMHQDAHEFLNFLLNELVdilekeskvvaepcensslkknsngpinvqlngtkkepvpTLVHKCFQGILTNETRCL 183
Cdd:cd02667  46 -FKGYQQQDSHELLRYLLDGLR----------------------------------------TFIDSIFGGELTSTIMCE 84
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSL----DIEQNSSITSCLKNFSSTETLNAEDKFFCDKCCslqEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:cd02667  85 SCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 260 YiEQLGRYKKLSYRVVFPLEL--------KLINTVDNSDLEYSLFAVLVHVGSGpNHGHYISLVKSHN-------HWLFF 324
Cdd:cd02667 162 Q-PRSANLRKVSRHVSFPEILdlapfcdpKCNSSEDKSSVLYRLYGVVEHSGTM-RSGHYVAYVKVRPpqqrlsdLTKSK 239
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 24756890 325 DDENVEMTDESmvQTFFGS---AQEFSGNT---DNGYILFYE 360
Cdd:cd02667 240 PAADEAGPGSG--QWYYISdsdVREVSLEEvlkSEAYLLFYE 279
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 6.18e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 141.09  E-value: 6.18e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYyaNNKSTGDvEDNMLTCLADLFSQISNQKKKTGVIAPKRFIQRLKkqnE 103
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL--NLPRLGD-SQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRP---P 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 IFRSYMHQDAHEFLNFLLNELvdilekeskvvaepcensslkknsngpinvqlngtkkepvPTLVHKCFQGILTNETRCL 183
Cdd:cd02664  75 WFTPGSQQDCSEYLRYLLDRL----------------------------------------HTLIEKMFGGKLSTTIRCL 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTDRDETFFDLSLDIeqnSSITSCLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKYIEQ 263
Cdd:cd02664 115 NCNSTSARTERFRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQK 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 264 LGRYKKLSYRVVFPLELKL--------INTVDNSDLE--------------YSLFAVLVHVGSGPNHGHYISLVK----- 316
Cdd:cd02664 192 THVREKIMDNVSINEVLSLpvrvesksSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtda 271
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24756890 317 -SHNH----------------WLFFDDENVEMTDESMVQ--TFFGSaqefsgnTDNGYILFYE 360
Cdd:cd02664 272 dSTGQecpepkdaeendesknWYLFNDSRVTFSSFESVQnvTSRFP-------KDTPYILFYE 327
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 6.00e-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 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: 132.45  E-value: 6.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNKSTGDVEDNMLTCLADLFSQISnqkKKTGVIAPKRFIQRL----- 98
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMD---KKQEPVPPIEFLQLLrmafp 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  99 ---KKQNEIFrsYMHQDAHEFLNFLLNELVDILEKESKvvaepcENSSLKKNSNGPINVQLNGTKKEPVptlvhkcfqgi 175
Cdd:cd02657  78 qfaEKQNQGG--YAQQDAEECWSQLLSVLSQKLPGAGS------KGSFIDQLFGIELETKMKCTESPDE----------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 176 ltnetrclrcETVTDRDETFFDLSLDIEQN-SSITSCLKnfsstETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIH 254
Cdd:cd02657 139 ----------EEVSTESEYKLQCHISITTEvNYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQ 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 255 LKRFKYIEQLGRYKKLSYRVVFPLELKLINTVDNSDLeYSLFAVLVHVGSGPNHGHYISLVKS--HNHWLFFDDENVEMT 332
Cdd:cd02657 204 FVRFFWKRDIQKKAKILRKVKFPFELDLYELCTPSGY-YELVAVITHQGRSADSGHYVAWVRRknDGKWIKFDDDKVSEV 282
                       330       340
                ....*....|....*....|....*...
gi 24756890 333 DESMVQTFFGsaqefSGNTDNGYILFYE 360
Cdd:cd02657 283 TEEDILKLSG-----GGDWHIAYILLYK 305
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 6.82e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 116.27  E-value: 6.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREQLLEYYanNKSTGDVED--NMLTC----LAD-LFSQ---ISNQKKKTGV----- 88
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLE--NKFPSDVVDpaNDLNCqlikLADgLLSGrysKPASLKSENDpyqvg 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  89 IAPKRFIQRLKKQNEIFRSYMHQDAHEFLNFLLnelvDILEKESKvvaepcenSSLKKNsngPINVqlngtkkepvptlv 168
Cdd:cd02658  79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLI----DKLDRESF--------KNLGLN---PNDL-------------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 169 hkcFQGILTNETRCLRCETVTDRDETFFDLSLDIE--------------QNSSITSCLKNFSSTETLnaedKFFCDKCCS 234
Cdd:cd02658 130 ---FKFMIEDRLECLSCKKVKYTSELSEILSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTCKE 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 235 LQEAQKRMKIKKPPNILVIHLKRFKYIEQlGRYKKLSYRVVFPLELKLINtvdnsdleYSLFAVLVHVGSGPNHGHYISL 314
Cdd:cd02658 203 KTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPKKLDVPIDVPEELGPGK--------YELIAFISHKGTSVHSGHYVAH 273
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 24756890 315 VK----SHNHWLFFDDENVemtdesmvqtffGSAQEFSGNTDNGYILFYE 360
Cdd:cd02658 274 IKkeidGEGKWVLFNDEKV------------VASQDPPEMKKLGYIYFYQ 311
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
24-329 2.03e-28

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 315986 [Multi-domain]  Cd Length: 295  Bit Score: 112.12  E-value: 2.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890    24 GLENFGNTCYCNSVLQALYFCVPFREQLLeyyaNNKSTGDVEDNMLTC-LADLFSQISNQKKKTGVIApkRFIQRLKKQN 102
Cdd:pfam13423   2 GLENHLDNSYLNALLQLYFFIPDLFEAIL----GHSFDECPPENCLLCeLGFLFDMLDKSNGQNCQAT--NFLRTFSTIP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   103 EIFRSYMHQDAHEFLNFLLNELvdILEKESKVVAEPCENSSLKKNsngpinvqlngtkkepvpTLVHKCFQGILTNETRC 182
Cdd:pfam13423  76 EAAALGLQQDIQEANRFILEQL--SLPLLTLKPSIENRRDSSEAE------------------SQLSELFGTGLINSIRC 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   183 LRCETVTDRDETFFDLSL---DIEQNSSITSCLKNFSSTETlnaEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:pfam13423 136 ISCNNESVKEESTLTVELpypPSEKGQNFSNILKSSIRREK---IVTIWCSSCNKYQPVLIRKTFVSLPPILGICLKRYS 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   260 YIEQLGRyKKLSYRVVFPLELKL---------INTVDNSDLEYSLFAVLVHVGSGPNHGHYISLV----KSHN-HWLFFD 325
Cdd:pfam13423 213 EKDNFWA-VRLNLFVDIPLEINMphfiqddeqNERPLSGLFKYELQGVVCHIGDSLTSGHLVSFIrvapSSENsQWYLFN 291

                  ....
gi 24756890   326 DENV 329
Cdd:pfam13423 292 DFLV 295
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
22-342 8.94e-27

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 111.89  E-value: 8.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   22 YFGLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNKSTgdvEDNMLTCLADLFSQISNQKKKTGVIapkrfiqRLKKQ 101
Cdd:COG5077  193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRG---RDSVALALQRLFYNLQTGEEPVDTT-------ELTRS 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  102 N--EIFRSYMHQDAHEFlnfllnelvdilekeSKVVAEPCENSslkknsngpinvqlngTKKEPVPTLVHKCFQGILTNE 179
Cdd:COG5077  263 FgwDSDDSFMQHDIQEF---------------NRVLQDNLEKS----------------MRGTVVENALNGIFVGKMKSY 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  180 TRCLRCETVTDRDETFFDLSLDIEQNSSITSCLKNFSSTETLNAEDKFFCDKcCSLQEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:COG5077  312 IKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFE 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  260 YIEQLGRYKKLSYRVVFPLELKLINTVD-------NSDLEYSLFAVLVHVGSGPNhGHYISLVKSH--NHWLFFDDENV- 329
Cdd:COG5077  391 YDFERDMMVKINDRYEFPLEIDLLPFLDrdadkseNSDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFDDTRVt 469
                        330
                 ....*....|...
gi 24756890  330 EMTDESMVQTFFG 342
Cdd:COG5077  470 RATEKEVLEENFG 482
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-360 5.88e-26

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: 103.99  E-value: 5.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQALYFCVPFREqlleyyannkstgdvednmltcladlfsqisnqkkktgviapkrFIQRLKKQne 103
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIE--------------------------------------------YLEEFLEQ-- 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 104 ifrsymhQDAHEFLNFLLNELvdilekeSKVVAEPcensslkknsngpinvqlngtkkepvptlvhkcFQGILTNETRCL 183
Cdd:cd02662  35 -------QDAHELFQVLLETL-------EQLLKFP---------------------------------FDGLLASRIVCL 67
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 184 RCETVTD-RDETFFDLSLDIEQNSSIT-----SCLKNFSSTETLnaeDKFFCDKCcslqeaqkRMKIKKPPNILVIHLKR 257
Cdd:cd02662  68 QCGESSKvRYESFTMLSLPVPNQSSGSgttleHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHLSR 136
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 258 FKYIEQlGRYKKLSYRVVFPLELklintvdnSDLEYSLFAVLVHVGSgPNHGHYISLVKS-------------------- 317
Cdd:cd02662 137 SVFDGR-GTSTKNSCKVSFPERL--------PKVLYRLRAVVVHYGS-HSSGHYVCYRRKplfskdkepgsfvrmregps 206
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 24756890 318 --HNHWLFFDDENVEMTDESMVQTfFGSAqefsgntdngYILFYE 360
Cdd:cd02662 207 stSHPWWRISDTTVKEVSESEVLE-QKSA----------YMLFYE 240
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
22-337 9.19e-22

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: 95.85  E-value: 9.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  22 YFGLENFGNTCYCNSVLQALYFCVPFREQLLEyYANNKSTGDVEDNMLTCLADLFSQISNQKKKTGVIAPKRFIQRLKKQ 101
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRNFFLL-YENYENIKDRKSELVKRLSELIRKIWNPRNFKGHVSPHELLQAVSKV 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 102 NEIFRSYMHQ-DAHEFLNFLLNelvdilekeskvvaepcensSLKKnsngpinvQLNGTKKePVPTLVHKCFQGILTNET 180
Cdd:cd02669 198 SKKKFSITEQsDPVEFLSWLLN--------------------TLHK--------DLGGSKK-PNSSIIHDCFQGKVQIET 248
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 181 RCLRCETVTD---------------RDETFFDLSLD-----IEQNSSITSCLKNFSSTETLnaeDKFFCDKCCSLQEAQK 240
Cdd:cd02669 249 QKIKPHAEEEgskdkffkdsrvkktSVSPFLLLTLDlppppLFKDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLK 325
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 241 RMKIKKPPNILVIHLKRF-KYIEQLGRYKKLsyrVVFPLELKLINTVDNSDLE-------YSLFAVLVHVGSGPNHGHYI 312
Cdd:cd02669 326 RYLISRLPKYLIFHIKRFsKNNFFKEKNPTI---VNFPIKNLDLSDYVHFDKPslnlstkYNLVANIVHEGTPQEDGTWR 402
                       330       340
                ....*....|....*....|....*..
gi 24756890 313 SLV--KSHNHWLFFDDENVEMTDESMV 337
Cdd:cd02669 403 VQLrhKSTNKWFEIQDLNVKEVLPQLI 429
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
211-360 6.76e-21

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 94.18  E-value: 6.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 211 CLKNFSSTETLNAEDKFFCDKCCSLQEAQKRMKIKKPPNILVIHLKRFKYieQLGRYKKLSYRVVFPLELKLIN----TV 286
Cdd:COG5560 680 CLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSS--VRSFRDKIDDLVEYPIDDLDLSgveyMV 757
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24756890 287 DNSDLEYSLFAVLVHVGsGPNHGHYISLVK--SHNHWLFFDDENVEMTDEsmVQTFFGSAqefsgntdngYILFYE 360
Cdd:COG5560 758 DDPRLIYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRITEVDP--EDSVTSSA----------YVLFYR 820
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-360 8.40e-19

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: 84.50  E-value: 8.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  25 LENFGNTCYCNSVLQALyfcvpfreqlleyyannKSTGDVednmltcladlfsqisnqkkktgviapkrfiqrlkkqNEI 104
Cdd:cd02673   2 LVNTGNSCYFNSTMQAL-----------------SSIGKI-------------------------------------NTE 27
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 105 FRSYMHQDAHEFLNFLLNELVDILEKESKvvaepcenssLKKNSNGPInVQLNgtkkepvPTLVHKcfqgiLTNETR--C 182
Cdd:cd02673  28 FDNDDQQDAHEFLLTLLEAIDDIMQVNRT----------NVPPSNIEI-KRLN-------PLEAFK-----YTIESSyvC 84
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 183 LRC---ETVTDRDeTFFDLSLDIEQNSSITSCLKNFSSTETLNAEdkffCDKCcSLQEAQKRMKIKKPPNILVIHLKRFK 259
Cdd:cd02673  85 IGCsfeENVSDVG-NFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYK 158
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 260 YIEQLGRYKKLSYRVVFPLELKLINtvdnsdleYSLFAVLVHVGSGPNHGHYISLVKS---HNHWLFFDDENVEMTDESM 336
Cdd:cd02673 159 LRIATSDYLKKNEEIMKKYCGTDAK--------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEIRPVSKND 230
                       330       340
                ....*....|....*....|....
gi 24756890 337 VQTFFGSAqefsgntdnGYILFYE 360
Cdd:cd02673 231 VSTNARSS---------GYLIFYD 245
UBP14 COG5207
Uncharacterized Zn-finger protein, UBP-type [General function prediction only];
4-260 2.95e-11

Uncharacterized Zn-finger protein, UBP-type [General function prediction only];


Pssm-ID: 227532 [Multi-domain]  Cd Length: 749  Bit Score: 64.70  E-value: 2.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890   4 ASSRLEKALGEQFPEgeRYFGLENFGNTCYCNSVLQALYFCVPFREQLLEYYANNKSTGDVEDNMLTC-LADLFSQISNQ 82
Cdd:COG5207 287 EKKRAPESKGESVPS--PYVGLINLGNSCYLSSVIQSLVGYAVSKEEFDLLQHFEICYMKNPLECLFCqLMKLLSKMKET 364
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  83 KKKTGV--IAPKRFIQRLKKQNEIFRSYMHQDAHEFLNFLLNElvdILEKESkvvaepcenSSLKKnsngpinvqlngtk 160
Cdd:COG5207 365 PDNEYVngISPLDFKMLIGQDHPEFGKFAQQDAHEFLLFLLEK---IRKGER---------SYLIP-------------- 418
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 161 kePVPTLvhkcFQGILTNETRCLRCETVTDRDETFFDLSLDIEQN---SSITSCLKNFSSTETLnaedKFFCDKCCSLQE 237
Cdd:COG5207 419 --PITSL----FEFEVERRLSCSGCMDVSYSYESMLMICIFLEGNdepQDIRKSVEAFFLPDTI----EWSCENCKGKKK 488
                       250       260
                ....*....|....*....|...
gi 24756890 238 AQKRMKIKKPPNILVIHLKRFKY 260
Cdd:COG5207 489 ASRKPFIKSLPKYLILQVGRYSL 511
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
24-359 1.70e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 52.11  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890  24 GLENFGNTCYCNSVLQaLYFCV-PFREQLLEYyanNKSTGDVEDNMLTCLADLFSQISNQKKKTGViapkRFIQRLKkqn 102
Cdd:cd02666   3 GLDNIGNTCYLNSLLQ-YFFTIkPLRDLVLNF---DESKAELASDYPTERRIGGREVSRSELQRSN----QFVYELR--- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 103 EIFRSYMHQDAH------EFLNFLLNElVDILEKESKVVAEpcENSSLKKNSNGPINVQLNGTKKEpvPTLVHKCFQGIL 176
Cdd:cd02666  72 SLFNDLIHSNTRsvtpskELAYLALRQ-QDVTECIDNVLFQ--LEVALEPISNAFAGPDTEDDKEQ--SDLIKRLFSGKT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 177 ---TNETRCLRCETVTDRDETFFDLSLDIEQNSSITSCLKnfSSTETLNAEDKFFCDKccSLQEAQKRMKIkkppnilVI 253
Cdd:cd02666 147 kqqLVPESMGNQPSVRTKTERFLSLLVDVGKKGREIVVLL--EPKDLYDALDRYFDYD--SLTKLPQRSQV-------QA 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 254 HLKRFKYIEQLG---RYKKLSYRVVFPLELKLINTVD-------------NSDLE----------YSLFAVLVHVGSGpN 307
Cdd:cd02666 216 QLAQPLQRELISmdrYELPSSIDDIDELIREAIQSESslvrqaqnelaelKHEIEkqfddlksygYRLHAVFIHRGEA-S 294
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 24756890 308 HGHYISLVKSH--NHWLFFDDENVEMTDESMVQTFfgsaqeFSGNTDNGYILFY 359
Cdd:cd02666 295 SGHYWVYIKDFeeNVWRKYNDETVTVVPASEVFLF------TLGNTATPYFLVY 342
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
244-360 7.36e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 49.45  E-value: 7.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 244 IKKPPNILVIHLKRFKYIEqlGRYKKLSYRVVFPLELKLINTVDNSDLEY-------------------------SLFAV 298
Cdd:cd02670  95 FAKAPSCLIICLKRYGKTE--GKAQKMFKKILIPDEIDIPDFVADDPRACskcqlecrvcyddkdfsptcgkfklSLCSA 172
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24756890 299 LVHVGSGPNHGHYISLVKS-------------HNHWLFFDDenveMTDESMVQTffGSAQEFSGNTDNGYILFYE 360
Cdd:cd02670 173 VCHRGTSLETGHYVAFVRYgsysltetdneayNAQWVFFDD----MADRDGVSN--GFNIPAARLLEDPYMLFYQ 241
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
239-359 2.29e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 44.86  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 239 QKRMKIKKPPnILVIHLKRFKYIEqlGRYKKLSYRVVFPLELKLINtvdnsdleYSLFAVLVHVGSGpNHGHYIS--LVK 316
Cdd:cd02665 121 QERWFTELPP-VLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVP--------YELHAVLVHEGQA-NAGHYWAyiYKQ 188
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24756890 317 SHNHWLFFDDENVEMTD-ESMVQTFFGSAQEFSgntdnGYILFY 359
Cdd:cd02665 189 SRQEWEKYNDISVTESSwEEVERDSFGGGRNPS-----AYCLMY 227
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
168-335 9.86e-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: 40.19  E-value: 9.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 168 VHKCFQGILTNETRC------LRCETVTDRDETFFDLSLD-----IEQNSSITSCLKNFSsteTLNAEDKFFCDKCCSLQ 236
Cdd:cd02672  68 LIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPlgstkTSKESTFLQLLKRSL---DLEKVTKAWCDTCCKYQ 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24756890 237 EAQKRMKIKKPPNI----LVIHLKRFKYIE-----QLGRYKKLSYRVVFPLE--LKLINTVDNSDL-EYSLFAVLVHVGS 304
Cdd:cd02672 145 PLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvVLPSGKVMQNKVSPKAIdhDKLVKNRGQESIyKYELVGYVCEIND 224
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24756890 305 GPNHGHYISLV------KSHNHWLFFDDENVEMTDES 335
Cdd:cd02672 225 SSRGQHNVVFVikvneeSTHGRWYLFNDFLVTPVSEL 261
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH