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Conserved domains on  [gi|7300926|gb|AAF56066|]
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Ubiquitin-specific protease 12/46 [Drosophila melanogaster]

Protein Classification

Peptidase_C19G domain-containing protein (domain architecture ID 10119250)

Peptidase_C19G domain-containing protein

Graphical summary

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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 ...
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 7300926   25 GLVNFGNTCYSNSVLQALYFckpfrekvleykaknkrpkETLLSCLADLFYSIATQKKKVGSIAPKKFITRLRKEKEEFD 104
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF-------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFD 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  105 NYMQQDAHEFLNFLINHINEIILAERNAGPSNGNpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02663  62 NYMHQDAHEFLNFLLNEIAEILDAERKAEKANRK---------------------------------------------- 95
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttpiisgnGTGTNGANSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNTSI 264
Cdd:cd02663  96 --------------------------LNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSI 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  265 THCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLFNTSDD 344
Cdd:cd02663 150 TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFNTTDD 229
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7300926  345 AVNPDRLYDLTAVVIHCGSGPNRGHYISIVKSHGLWLLFDDDMVDKIEASTIEDFYGltsdIHKSSETGYILFYQ 419
Cdd:cd02663 230 AENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEFFG----DSPNQATAYVLFYQ 300
 
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 7300926   25 GLVNFGNTCYSNSVLQALYFckpfrekvleykaknkrpkETLLSCLADLFYSIATQKKKVGSIAPKKFITRLRKEKEEFD 104
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF-------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFD 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  105 NYMQQDAHEFLNFLINHINEIILAERNAGPSNGNpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02663  62 NYMHQDAHEFLNFLLNEIAEILDAERKAEKANRK---------------------------------------------- 95
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttpiisgnGTGTNGANSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNTSI 264
Cdd:cd02663  96 --------------------------LNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSI 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  265 THCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLFNTSDD 344
Cdd:cd02663 150 TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFNTTDD 229
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7300926  345 AVNPDRLYDLTAVVIHCGSGPNRGHYISIVKSHGLWLLFDDDMVDKIEASTIEDFYGltsdIHKSSETGYILFYQ 419
Cdd:cd02663 230 AENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEFFG----DSPNQATAYVLFYQ 300
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
24-418 1.23e-80

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 250.38  E-value: 1.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926     24 FGLVNFGNTCYSNSVLQALYFCKPFREKVLEY---KAKNKRPKETLLSC-LADLFYSIATQKKKvGSIAPKKFITRLRKE 99
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRIsplSEDSRYNKDINLLCaLADLFKALQSEKKS-SSVSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    100 KEEFDNYMQQDAHEFLNFLINHINEIilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngns 179
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHED------------------------------------------------------ 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    180 snstgsLNANTSvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVD 259
Cdd:pfam00443 106 ------LNGKHS--------------------------TENESLITDLFRGQLKSRLKCLNCGKESYTFEPFLDLSLPIP 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    260 QNTS--ITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNrhIKVSHRVVFPLELR 337
Cdd:pfam00443 154 SLKNydLQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFSYNRSTW--EKLNTEVEFPEELD 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    338 LFNTSDDAVNPD----RLYDLTAVVIHCGSgPNRGHYISIVKSH--GLWLLFDDDMVDKIEASTIEdfygltsdihksSE 411
Cdd:pfam00443 232 LSEYLAEGLDEKevepTKYRLVAVVVHSGS-LSSGHYIAYIKKYenGRWYKFDDEKVTEVDEEEVL------------NK 298

                  ....*..
gi 7300926    412 TGYILFY 418
Cdd:pfam00443 299 SAYILFY 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
15-419 4.20e-32

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


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 125.91  E-value: 4.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   15 DLFPPNehyfGLVNFGNTCYSNSVLQALYFCK----PFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKKVG--SIA 88
Cdd:COG5533  67 DNLPPN----GLRNKGNTCYMNCALQCLLSIGdlntMLQGRFYLQNINTDFPRGKPGSNAFKQFIALYETPGCHGpkSIS 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   89 PKKFITRLRKEKEEFDNYMQQDAHEFLNFLINHINEiilaernagPSNGNpkatnqggstsamassiaskssstsnsnsn 168
Cdd:COG5533 143 PRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHE---------DLNGN------------------------------ 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  169 snsttnsngnsSNSTGSLNANTSVLDASGSLTATTTPIISGNgtgtNGANSEPTWVHEIFQGILTSETRCLNCETVSSKD 248
Cdd:COG5533 184 -----------KSRSPILELKDEFEEVREELPLSHFSHHEWN----LHLRSNKSLVAKTFFGQDKSRLQCEACNYTSTTI 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  249 ENFFDLQVDVDQ--NTSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHI-- 324
Cdd:COG5533 249 AMFSTLLVPPYEvvQLGLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRKRMEILVLPDVLIIHISRFHISVMGRKKIdt 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  325 ------KVSHRVVFPLelrLFNTSDDAvnPDRLYDLTAVVIHCGSgPNRGHYISIVKSHGLWLLFDDDMVDKIEastied 398
Cdd:COG5533 329 pqgwknTASVEVNVTL---LFNNGIGY--IPRKYSLLGVVCHNGT-LNGGHYFSEVKRSGTWNVYDDSQVRKGS------ 396
                       410       420
                ....*....|....*....|.
gi 7300926  399 fyGLTSDIHKSSetgYILFYQ 419
Cdd:COG5533 397 --RTTSGSHPSS---YILFYT 412
 
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 7300926   25 GLVNFGNTCYSNSVLQALYFckpfrekvleykaknkrpkETLLSCLADLFYSIATQKKKVGSIAPKKFITRLRKEKEEFD 104
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYF-------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENELFD 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  105 NYMQQDAHEFLNFLINHINEIILAERNAGPSNGNpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02663  62 NYMHQDAHEFLNFLLNEIAEILDAERKAEKANRK---------------------------------------------- 95
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttpiisgnGTGTNGANSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNTSI 264
Cdd:cd02663  96 --------------------------LNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSI 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  265 THCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLFNTSDD 344
Cdd:cd02663 150 TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFNTTDD 229
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7300926  345 AVNPDRLYDLTAVVIHCGSGPNRGHYISIVKSHGLWLLFDDDMVDKIEASTIEDFYGltsdIHKSSETGYILFYQ 419
Cdd:cd02663 230 AENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEFFG----DSPNQATAYVLFYQ 300
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
24-418 1.23e-80

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 334078 [Multi-domain]  Cd Length: 305  Bit Score: 250.38  E-value: 1.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926     24 FGLVNFGNTCYSNSVLQALYFCKPFREKVLEY---KAKNKRPKETLLSC-LADLFYSIATQKKKvGSIAPKKFITRLRKE 99
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQCLFSIPPFRDYLLRIsplSEDSRYNKDINLLCaLADLFKALQSEKKS-SSVSPKEFKKTLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    100 KEEFDNYMQQDAHEFLNFLINHINEIilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngns 179
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHED------------------------------------------------------ 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    180 snstgsLNANTSvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVD 259
Cdd:pfam00443 106 ------LNGKHS--------------------------TENESLITDLFRGQLKSRLKCLNCGKESYTFEPFLDLSLPIP 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    260 QNTS--ITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNrhIKVSHRVVFPLELR 337
Cdd:pfam00443 154 SLKNydLQDCLKAFTKEEILKGENMYYCPKCKGKCGAIKKLKISRLPPVLIIHLKRFSYNRSTW--EKLNTEVEFPEELD 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    338 LFNTSDDAVNPD----RLYDLTAVVIHCGSgPNRGHYISIVKSH--GLWLLFDDDMVDKIEASTIEdfygltsdihksSE 411
Cdd:pfam00443 232 LSEYLAEGLDEKevepTKYRLVAVVVHSGS-LSSGHYIAYIKKYenGRWYKFDDEKVTEVDEEEVL------------NK 298

                  ....*..
gi 7300926    412 TGYILFY 418
Cdd:pfam00443 299 SAYILFY 305
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
25-419 1.36e-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: 1.36e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFckpfrekvleykaknkrpketllscladlfysiatqkkkvgsiapkkfitrlrkekeefd 104
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  105 nyMQQDAHEFLNFLINHINEIILAERNAGPSNgnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02257  21 --EQQDAHEFLLFLLDKLHEELKKSSKRTSDS------------------------------------------------ 50
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNT-- 262
Cdd:cd02257  51 ---------------------------------SSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGlp 97
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  263 --SITHCLRCFSNTETLCSDNKFKCDnCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRhIKVSHRVVFPLELRLFN 340
Cdd:cd02257  98 qvSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTK-EKLNTKVSFPLELDLSP 175
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  341 ------TSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVK--SHGLWLLFDDDMVDKIEASTIEDFYGLTSdihksseT 412
Cdd:cd02257 176 ylsegeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdpSDGKWYKFNDDKVTEVSEEEVLEFGSLSS-------S 248

                ....*..
gi 7300926  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 2.49e-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: 2.49e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKA-KNKRPKETLLSCLADLFYSIATQKKKvGSIAPKKFITRLRKEKEEF 103
Cdd:cd02661   3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHsKDCCNEGFCMMCALEAHVERALASSG-PGSAPRIFSSNLKQISKHF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  104 DNYMQQDAHEFLNFLINHINEIILAERNAgpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnst 183
Cdd:cd02661  82 RIGRQEDAHEFLRYLLDAMQKACLDRFKK--------------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  184 gslnantsvLDASGSLTATTTpiisgngtgtnganseptWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQNTS 263
Cdd:cd02661 111 ---------LKAVDPSSQETT------------------LVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADS 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  264 ITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFK--YMEQFNRHIKvshrvvFPLELRLFNT 341
Cdd:cd02661 164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSnfRGGKINKQIS------FPETLDLSPY 237
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7300926  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 6.54e-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: 6.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSC-LADLFYSIATQKKKVgsIAPKKFITRLRKEKE 101
Cdd:cd02659   2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLaLQRLFLFLQLSESPV--KTTELTDKTRSFGWD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  102 EFDNYMQQDAHEFLNFLINHINEIIlaernagpsngnpKATNQggstsamassiaskssstsnsnsnsnsttnsngnssn 181
Cdd:cd02659  80 SLNTFEQHDVQEFFRVLFDKLEEKL-------------KGTGQ------------------------------------- 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  182 stgslnantsvldasgsltatttpiisgngtgtngansEPTwVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQN 261
Cdd:cd02659 110 --------------------------------------EGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGK 150
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  262 TSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLEL----- 336
Cdd:cd02659 151 KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELdmepy 230
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  337 ------RLFNTSDDAVNPDRLYDLTAVVIHCGSGPNrGHYISIVKS--HGLWLLFDDDMVDKIEASTIED------FYGL 402
Cdd:cd02659 231 tekglaKKEGDSEKKDSESYIYELHGVLVHSGDAHG-GHYYSYIKDrdDGKWYKFNDDVVTPFDPNDAEEecfggeETQK 309
                       410       420
                ....*....|....*....|....*
gi 7300926  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 1.58e-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: 1.58e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLA--------DLFYSIATQkkkvgsiaPKKFITRL 96
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLScamdeifqEFYYSGDRS--------PYGPINLL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   97 R---KEKEEFDNYMQQDAHEFLNFLINHINEiiLAERNAGPSNGNpkatnqggstsamassiaskssstsnsnsnsnstt 173
Cdd:cd02660  74 YlswKHSRNLAGYSQQDAHEFFQFLLDQLHT--HYGGDKNEANDE----------------------------------- 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  174 nsngnssnstgslnantsvldasgsltatttpiisgngtgtngaNSEPTWVHEIFQGILTSETRCLNCETVSSKDENFFD 253
Cdd:cd02660 117 --------------------------------------------SHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  254 LQVDVDQNT---------------SITHCLRCFSNTETLCSDNkFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYmE 318
Cdd:cd02660 153 LSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEH-S 230
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  319 QFNRHIKVSHRVVFPLELRL---------FNTSDDAVNPDRLYDLTAVVIHCGSgPNRGHYISIVKSH-GLWLLFDDDMV 388
Cdd:cd02660 231 LNKTSRKIDTYVQFPLELNMtpytsssigDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQGdGQWFKFDDAMI 309
                       410       420       430
                ....*....|....*....|....*....|
gi 7300926  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 2.01e-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: 2.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  228 FQGILTSETRCLNCETVSSKDENFFDLQVDVDQNT------SITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVK 301
Cdd:cd02674  44 FQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTIS 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  302 KLPMILALHLKRFKYmeQFNRHIKVSHRVVFPLE---LRLFNTSDDAVNPDRlYDLTAVVIHCGSGpNRGHYISIVKS-- 376
Cdd:cd02674 124 RLPKVLIIHLKRFSF--SRGSTRKLTTPVTFPLNdldLTPYVDTRSFTGPFK-YDLYAVVNHYGSL-NGGHYTAYCKNne 199
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 7300926  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 6.23e-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: 6.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLA--DLFYSIAtqkkkvGSIAPKKFITRLRKEKEE 102
Cdd:cd02671  26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDEL------ANQAPRRLLNALREVNPM 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  103 FDNYMQQDAHEFLNFLINHINEIilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssns 182
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQEL--------------------------------------------------------- 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  183 tgslnantsvldasgsltatttpiisgngtgtnganseptwVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDV---- 258
Cdd:cd02671 123 -----------------------------------------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVqese 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  259 ----DQNTSITHCLRC-----------FSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRF----KYMEQ 319
Cdd:cd02671 162 lsksEESSEISPDPKTemktlkwaisqFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFaangSEFDC 241
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  320 FNRHIKVSHRVVFPLELRLFNTSDDAVNPDrlYDLTAVVIHCGSGPNRGHYISIVKshglWLLFDDdmvDKIEASTIEDF 399
Cdd:cd02671 242 YGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAYVR----WLLFDD---SEVKVTEEKDF 312
                       410
                ....*....|....*....
gi 7300926  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 5.20e-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: 5.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEY-----------KAKNKRPKETLLSCLADLFYSIATQKKKVgsIAPKKFI 93
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECnstedaelknmPPDKPHEPQTIIDQLQLIFAQLQFGNRSV--VDPSGFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   94 TRLRkekeeFDNYMQQDAHEFLNFLINHINEIILaernagpSNGNPKATNqggstsamassiaskssstsnsnsnsnstt 173
Cdd:cd02668  79 KALG-----LDTGQQQDAQEFSKLFLSLLEAKLS-------KSKNPDLKN------------------------------ 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  174 nsngnssnstgslnantsvldasgsltatttpiisgngtgtnganseptWVHEIFQGILTSETRCLNCETVSSKDENFFD 253
Cdd:cd02668 117 -------------------------------------------------IVQDLFRGEYSYVTQCSKCGRESSLPSKFYE 147
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  254 LQVDVDQNTSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFP 333
Cdd:cd02668 148 LELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFP 227
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  334 LELRLFNTSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVK--SHGLWLLFDDDMVDKIEASTIEDfyGLTSDIHK--- 408
Cdd:cd02668 228 EILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdeQTGEWYKFNDEDVEEMPGKPLKL--GNSEDPAKprk 305
                       410
                ....*....|....*...
gi 7300926  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 6.61e-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: 6.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKKVGSiAPKKFITRLRKEKeeFD 104
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEA-PPDYFLEASRPPW--FT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  105 NYMQQDAHEFLNFLINHINeiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02664  78 PGSQQDCSEYLRYLLDRLH------------------------------------------------------------- 96
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttpiisgngtgtngansepTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVdqnTSI 264
Cdd:cd02664  97 -------------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSV 136
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  265 THCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRL------ 338
Cdd:cd02664 137 QDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLpvrves 216
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  339 -------------FNTSDDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVKS----------------------HGLWLLF 383
Cdd:cd02664 217 kssesplekkeeeSGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLF 296
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 7300926  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 3.11e-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: 3.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEykaknkRPKEtLLSCLadlfysiatqkkkvgsiapkkfitrlRKEKEEFD 104
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------TPKE-LFSQV--------------------------CRKAPQFK 47
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  105 NYMQQDAHEFLNFLINHINeiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02667  48 GYQQQDSHELLRYLLDGLR------------------------------------------------------------- 66
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttpiisgngtgtngansepTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQ----VDVDQ 260
Cdd:cd02667  67 -------------------------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSlprsDEIKS 109
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  261 NTSITHCLRCFSNTETLCSDNKFKCDNCCsyqEAQKRMRVKKLPMILALHLKRFKyMEQFNRHIKVSHRVVFP--LELRL 338
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQ-QPRSANLRKVSRHVSFPeiLDLAP 185
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  339 FNTSDDAVNPDR---LYDLTAVVIHCGSGpNRGHYISIVKSHGLWLLFDDDMVDKIEASTIED-----FYGLTSDIHKSS 410
Cdd:cd02667 186 FCDPKCNSSEDKssvLYRLYGVVEHSGTM-RSGHYVAYVKVRPPQQRLSDLTKSKPAADEAGPgsgqwYYISDSDVREVS 264
                       410
                ....*....|....*
gi 7300926  411 ET------GYILFYQ 419
Cdd:cd02667 265 LEevlkseAYLLFYE 279
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ...
15-419 4.20e-32

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


Pssm-ID: 227820 [Multi-domain]  Cd Length: 415  Bit Score: 125.91  E-value: 4.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   15 DLFPPNehyfGLVNFGNTCYSNSVLQALYFCK----PFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKKVG--SIA 88
Cdd:COG5533  67 DNLPPN----GLRNKGNTCYMNCALQCLLSIGdlntMLQGRFYLQNINTDFPRGKPGSNAFKQFIALYETPGCHGpkSIS 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   89 PKKFITRLRKEKEEFDNYMQQDAHEFLNFLINHINEiilaernagPSNGNpkatnqggstsamassiaskssstsnsnsn 168
Cdd:COG5533 143 PRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHE---------DLNGN------------------------------ 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  169 snsttnsngnsSNSTGSLNANTSVLDASGSLTATTTPIISGNgtgtNGANSEPTWVHEIFQGILTSETRCLNCETVSSKD 248
Cdd:COG5533 184 -----------KSRSPILELKDEFEEVREELPLSHFSHHEWN----LHLRSNKSLVAKTFFGQDKSRLQCEACNYTSTTI 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  249 ENFFDLQVDVDQ--NTSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHI-- 324
Cdd:COG5533 249 AMFSTLLVPPYEvvQLGLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRKRMEILVLPDVLIIHISRFHISVMGRKKIdt 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  325 ------KVSHRVVFPLelrLFNTSDDAvnPDRLYDLTAVVIHCGSgPNRGHYISIVKSHGLWLLFDDDMVDKIEastied 398
Cdd:COG5533 329 pqgwknTASVEVNVTL---LFNNGIGY--IPRKYSLLGVVCHNGT-LNGGHYFSEVKRSGTWNVYDDSQVRKGS------ 396
                       410       420
                ....*....|....*....|.
gi 7300926  399 fyGLTSDIHKSSetgYILFYQ 419
Cdd:COG5533 397 --RTTSGSHPSS---YILFYT 412
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-418 6.96e-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: 6.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKET---LLSCLADLFysiATQKKKVGSIAPKKFITRLRK--- 98
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSsdnLTNALRDLF---DTMDKKQEPVPPIEFLQLLRMafp 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   99 ---EKEEFDNYMQQDAHEFLNFLinhineiilaernagpsngnpkatnqggstsamassiaskssstsnsnsnsnsttns 175
Cdd:cd02657  78 qfaEKQNQGGYAQQDAEECWSQL--------------------------------------------------------- 100
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  176 ngnssnstgsLNANTSVLDasgsltatttpiisgngtgtnGANSEPTWVHEIFQGILTSETRCLNCETV-SSKDENFFDL 254
Cdd:cd02657 101 ----------LSVLSQKLP---------------------GAGSKGSFIDQLFGIELETKMKCTESPDEeEVSTESEYKL 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  255 QVDVDQNTSITH----CLRCFSNTETLCSDnkfKCDNCCSYQeaqKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRV 330
Cdd:cd02657 150 QCHISITTEVNYlqdgLKKGLEEEIEKHSP---TLGRDAIYT---KTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKV 223
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  331 VFPLELRLFntsdDAVNPDRLYDLTAVVIHCGSGPNRGHYISIVKS--HGLWLLFDDDMVDKIEASTIEDFYGlTSDIHk 408
Cdd:cd02657 224 KFPFELDLY----ELCTPSGYYELVAVITHQGRSADSGHYVAWVRRknDGKWIKFDDDKVSEVTEEDILKLSG-GGDWH- 297
                       410
                ....*....|
gi 7300926  409 sseTGYILFY 418
Cdd:cd02657 298 ---IAYILLY 304
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
23-401 8.10e-26

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 110.35  E-value: 8.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKKVGSiapkkfiTRLRKEK-- 100
Cdd:COG5077  193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDT-------TELTRSFgw 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   101 EEFDNYMQQDAHEFLNFLINHIneiilaERNAgpsngnpkatnqggstsamassiaskssstsnsnsnsnsttnsngnss 180
Cdd:COG5077  266 DSDDSFMQHDIQEFNRVLQDNL------EKSM------------------------------------------------ 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   181 nstgslnANTSVLDAsgsltatttpiisgngtgtnganseptwVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQ 260
Cdd:COG5077  292 -------RGTVVENA----------------------------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   261 NTSITHCLRCFSNTETLCSDNKFKCDNCcSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLF- 339
Cdd:COG5077  337 MKNLQESFRRYIQVETLDGDNRYNAEKH-GLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLp 415
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7300926   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 7.84e-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: 7.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   25 GLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPK-------ETLLSCLADLF----YSIATQKKKVGS-----IA 88
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVvdpandlNCQLIKLADGLlsgrYSKPASLKSENDpyqvgIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   89 PKKFITRLRKEKEEFDNYMQQDAHEFLNFLINHIneiilaERNAGPSNGnpkatnqggstsamassiaskssstsnsnsn 168
Cdd:cd02658  81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKL------DRESFKNLG------------------------------- 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  169 snsttnsngnssnstgslnantsvldasgsltatttpiisgngtgtnganSEPTwvhEIFQGILTSETRCLNCETVSSKD 248
Cdd:cd02658 124 --------------------------------------------------LNPN---DLFKFMIEDRLECLSCKKVKYTS 150
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  249 ENFFDLQVDVD--------------QNTSITHCLRCFSNTETLcsdnKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRF 314
Cdd:cd02658 151 ELSEILSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  315 KYMEQFnRHIKVSHRVVFPLELRlfntsddavnPDRlYDLTAVVIHCGSGPNRGHYISIVK----SHGLWLLFDDdmvDK 390
Cdd:cd02658 227 QLLENW-VPKKLDVPIDVPEELG----------PGK-YELIAFISHKGTSVHSGHYVAHIKkeidGEGKWVLFND---EK 291
                       410       420
                ....*....|....*....|....*....
gi 7300926  391 IEASTIEDFygltsdiHKssETGYILFYQ 419
Cdd:cd02658 292 VVASQDPPE-------MK--KLGYIYFYQ 311
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
25-388 2.27e-21

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 315986 [Multi-domain]  Cd Length: 295  Bit Score: 93.25  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926     25 GLVNFGNTCYSNSVLQALYFCKPFREKVLeYKAKNKRPKETLLSC----LADLFYSIATQKKKVgsiapKKFITRLRKEK 100
Cdd:pfam13423   2 GLENHLDNSYLNALLQLYFFIPDLFEAIL-GHSFDECPPENCLLCelgfLFDMLDKSNGQNCQA-----TNFLRTFSTIP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    101 EEFDNYMQQDAHEFLNFLINhinEIILAERNAGPSNGNPKATNQGGstsamassiaskssstsnsnsnsnsttnsngnss 180
Cdd:pfam13423  76 EAAALGLQQDIQEANRFILE---QLSLPLLTLKPSIENRRDSSEAE---------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    181 nstgslnantsvldasgsltatttpiisgngtgtngansepTWVHEIFQGILTSETRCLNCETVSSKDENFFDLQVDVDQ 260
Cdd:pfam13423 119 -----------------------------------------SQLSELFGTGLINSIRCISCNNESVKEESTLTVELPYPP 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926    261 NTS---ITHCLRCFSNTETlcsDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRhIKVSHRVVFPLELR 337
Cdd:pfam13423 158 SEKgqnFSNILKSSIRREK---IVTIWCSSCNKYQPVLIRKTFVSLPPILGICLKRYSEKDNFWA-VRLNLFVDIPLEIN 233
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7300926    338 LFN-TSDDAVN-----PDRLYDLTAVVIHCGSGPNRGHYISIVK---SHGL--WLLFDDDMV 388
Cdd:pfam13423 234 MPHfIQDDEQNerplsGLFKYELQGVVCHIGDSLTSGHLVSFIRvapSSENsqWYLFNDFLV 295
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
263-421 2.05e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 87.63  E-value: 2.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  263 SIT--HCLRCFSNTETLCSDNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRhiKVSHRVVFP---LELR 337
Cdd:COG5560 674 TITlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYPiddLDLS 751
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  338 LFNTSDDavNPDRLYDLTAVVIHCGsGPNRGHYISIVK--SHGLWLLFDDDMVDKIEAstiedfygltSDIHKSSetGYI 415
Cdd:COG5560 752 GVEYMVD--DPRLIYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRITEVDP----------EDSVTSS--AYV 816

                ....*.
gi 7300926  416 LFYQSR 421
Cdd:COG5560 817 LFYRRK 822
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
228-419 8.48e-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: 8.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  228 FQGILTSETRCLNCETVSSKDENFFD---LQV---DVDQNTSITHCLRCFSNTETlCSDnkFKCDNCcsyQEAqkrmrVK 301
Cdd:cd02662  56 FDGLLASRIVCLQCGESSKVRYESFTmlsLPVpnqSSGSGTTLEHCLDDFLSTEI-IDD--YKCDRC---QTV-----IV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  302 KLPMILALHLKRFkymeQFNRHI---KVSHRVVFPLELrlfntsddavnPDRLYDLTAVVIHCGSgPNRGHYISIVKSHG 378
Cdd:cd02662 125 RLPQILCIHLSRS----VFDGRGtstKNSCKVSFPERL-----------PKVLYRLRAVVVHYGS-HSSGHYVCYRRKPL 188
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 7300926  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 1.13e-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: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   26 LVNFGNTCYSNSVLQALyfckpfrekvleykaknkrpketllscladlfysiatqkkkvgsiapkkfiTRLRKEKEEFDN 105
Cdd:cd02673   2 LVNTGNSCYFNSTMQAL---------------------------------------------------SSIGKINTEFDN 30
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  106 YMQQDAHEFLNFLINHINEIILAER-NAGPSNGNPKATNqggstsamassiaskssstsnsnsnsnsttnsngnssnstg 184
Cdd:cd02673  31 DDQQDAHEFLLTLLEAIDDIMQVNRtNVPPSNIEIKRLN----------------------------------------- 69
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  185 slnantsvldasgsltatttPIisgngtgtnganseptwvhEIFQGILTSETRCLNC--ETVSSKDENFFDLQV---DVD 259
Cdd:cd02673  70 --------------------PL-------------------EAFKYTIESSYVCIGCsfEENVSDVGNFLDVSMidnKLD 110
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  260 QNTSITHCLRCFSNTETLCSDnkfkcdncCSYQEAQKRMRVKKLPMILALHLKRFKYMEQFNRHIKVSHRVVFPLELRLF 339
Cdd:cd02673 111 IDELLISNFKTWSPIEKDCSS--------CKCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEIMKKYCGTDA 182
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  340 NtsddavnpdrlYDLTAVVIHCGSGPNRGHYISIVKS---HGLWLLFDDDMVDKIEASTIedfygltsdIHKSSETGYIL 416
Cdd:cd02673 183 K-----------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEIRPVSKNDV---------STNARSSGYLI 242

                ..
gi 7300926  417 FY 418
Cdd:cd02673 243 FY 244
UBP14 COG5207
Uncharacterized Zn-finger protein, UBP-type [General function prediction only];
23-124 3.54e-09

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


Pssm-ID: 227532 [Multi-domain]  Cd Length: 749  Bit Score: 58.54  E-value: 3.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYKAKNKRPKETLLSCLADLFYSIATQKKK------VGSIAPKKFITRL 96
Cdd:COG5207 303 YVGLINLGNSCYLSSVIQSLVGYAVSKEEFDLLQHFEICYMKNPLECLFCQLMKLLSKMKEtpdneyVNGISPLDFKMLI 382
                        90       100
                ....*....|....*....|....*...
gi 7300926   97 RKEKEEFDNYMQQDAHEFLNFLINHINE 124
Cdd:COG5207 383 GQDHPEFGKFAQQDAHEFLLFLLEKIRK 410
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
23-392 2.03e-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: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   23 YFGLVNFGNTCYSNSVLQALYFCKPFREKVLEYK--AKNKRPKETLLSCLADLFYSIATQKKKVGSIAPKKF---ITRLR 97
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnyENIKDRKSELVKRLSELIRKIWNPRNFKGHVSPHELlqaVSKVS 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926   98 KEKeeFDNYMQQDAHEFLNFLINHINeiilaernagpsngnpKATNQGGSTsamassiaskssstsnsnsnsnsttnsng 177
Cdd:cd02669 199 KKK--FSITEQSDPVEFLSWLLNTLH----------------KDLGGSKKP----------------------------- 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  178 nssnstgslnaNTSVLDAS--GSLTATTTPIISGNGTGTNGANseptwVHEIFQGILTSETRCLncetVSSKDENFFDLQ 255
Cdd:cd02669 232 -----------NSSIIHDCfqGKVQIETQKIKPHAEEEGSKDK-----FFKDSRVKKTSVSPFL----LLTLDLPPPPLF 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  256 VDVDQNTSITHclrcFSNTETLcsdNKFKCDNCCSYQEAQKRMRVKKLPMILALHLKRF-KYMEQFNRHIKVshrVVFPL 334
Cdd:cd02669 292 KDGNEENIIPQ----VPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFsKNNFFKEKNPTI---VNFPI 361
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7300926  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 1.54e-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: 1.54e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 7300926   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 8.32e-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: 8.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  224 VHEIFQGIL--TSETRCLN----CETVSSKDENFFDLQVDVD--QNTSITHCLRCFSNTETLCSDNKFKCDNCCSYQEAQ 295
Cdd:cd02672  68 LIQNFTRFLleTISQDQLGtpfsCGTSRNSVSLLYTLSLPLGstKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLE 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  296 KRMRVKKLPMI----LALHLKRFKYMEQFNRHIKVS-----HRVVFPLELRLFNTSDDAVNPDRLYDLTAVVIHCGSGPN 366
Cdd:cd02672 148 QTTSIRHLPDIlllvLVINLSVTNGEFDDINVVLPSgkvmqNKVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSR 227
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7300926  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 9.81e-05

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 43.28  E-value: 9.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7300926  301 KKLPMILALHLKRFKYMEQFNrhIKVSHRVVFPLELRL----------------------FNTSDDAVNPDRLYDLTAVV 358
Cdd:cd02670  96 AKAPSCLIICLKRYGKTEGKA--QKMFKKILIPDEIDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAV 173
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7300926  359 IHCGSGPNRGHYISIVK--SHGL-----------WLLFdDDMVDKIEAstiedFYGLTSDIHKSSETGYILFYQ 419
Cdd:cd02670 174 CHRGTSLETGHYVAFVRygSYSLtetdneaynaqWVFF-DDMADRDGV-----SNGFNIPAARLLEDPYMLFYQ 241
 
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.
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