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Conserved domains on  [gi|2184285241|ref|NP_001387723|]
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ubiquitin carboxyl-terminal hydrolase 28 isoform 30 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10119287)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-371 1.98e-91

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: 279.83  E-value: 1.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsyslpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 216
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLFS------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNG 296
Cdd:cd02665    21 ---------QQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2184285241 297 YRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIYMDRY 371
Cdd:cd02665    92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVPY 164
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 137-241 4.70e-10

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.


The actual alignment was detected with superfamily member cd02664:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 327  Bit Score: 61.35  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNvlencrshTEKRNIMFMqeLQYLFALMMGSNRKfvdPSAALDLL 216
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--------GDSQSVMKK--LQLLQAHLMHTQRR---AEAPPDYF 67

                          90       100
                  ....*....|....*....|....*...
gi 2184285241 217 KGAFRS---SEEQQQDVSEFTHKLLDWL 241
Cdd:cd02664    68 LEASRPpwfTPGSQQDCSEYLRYLLDRL 95
 
Name Accession Description Interval E-value
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-371 1.98e-91

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: 279.83  E-value: 1.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsyslpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 216
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLFS------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNG 296
Cdd:cd02665    21 ---------QQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2184285241 297 YRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIYMDRY 371
Cdd:cd02665    92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVPY 164
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
136-372 3.90e-31

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.94  E-value: 3.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 136 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSlpqNVLENCRSHTEkrnIMFMQELQYLF-ALMMGSNRKFVDPSAALD 214
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS---PLSEDSRYNKD---INLLCALRDLFkALQKNSKSSSVSPKMFKK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 215 LLKGAFRS-SEEQQQDVSEFTHKLLDWLEDAFqlavnVNSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET------- 286
Cdd:pfam00443  75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLS---CGEVSetfepfs 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 287 FGQYPLQVNGYRNLDECLEGAMVE-------GDVELLPSDHSVKYGQ---ERWFTKLPPVLTFELSRFEFNQSlgQPEKI 356
Cdd:pfam00443 147 DLSLPIPGDSAELKTASLQICFLQfskleelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKL 224

                         250
                  ....*....|....*.
gi 2184285241 357 HNKLEFPQIIYMDRYM 372
Cdd:pfam00443 225 NTEVEFPLELDLSRYL 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 136-377 6.58e-14

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 74.91  E-value: 6.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241  136 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVlsYSLPQNvlencrsHTEKRNIMFMQeLQYLFALMMGSNrkfvDPSAALDL 215
Cdd:COG5077    194 VGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTD-------HPRGRDSVALA-LQRLFYNLQTGE----EPVDTTEL 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241  216 LKGAFRSSEEQ--QQDVSEFTHKLLDWLEDafqlavnvNSPRNKSENPMVQLFYGTFLT--EGVREGKPFCNNETFGQYP 291
Cdd:COG5077    260 TRSFGWDSDDSfmQHDIQEFNRVLQDNLEK--------SMRGTVVENALNGIFVGKMKSyiKCVNVNYESARVEDFWDIQ 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241  292 LQVNGYRNLDECLEGAMvegDVELLPSDHsvKYGQERW----------FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLE 361
Cdd:COG5077    332 LNVKGMKNLQESFRRYI---QVETLDGDN--RYNAEKHglqdakkgviFESLPPVLHLQLKRFEYDFERDMMVKINDRYE 406

                          250       260
                   ....*....|....*....|
gi 2184285241  362 FPQII----YMDRYMYRSKE 377
Cdd:COG5077    407 FPLEIdllpFLDRDADKSEN 426
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-241 4.70e-10

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: 61.35  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNvlencrshTEKRNIMFMqeLQYLFALMMGSNRKfvdPSAALDLL 216
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--------GDSQSVMKK--LQLLQAHLMHTQRR---AEAPPDYF 67

                          90       100
                  ....*....|....*....|....*...
gi 2184285241 217 KGAFRS---SEEQQQDVSEFTHKLLDWL 241
Cdd:cd02664    68 LEASRPpwfTPGSQQDCSEYLRYLLDRL 95
 
Name Accession Description Interval E-value
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-371 1.98e-91

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: 279.83  E-value: 1.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsyslpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 216
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLFS------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNG 296
Cdd:cd02665    21 ---------QQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2184285241 297 YRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQslGQPEKIHNKLEFPQIIYMDRY 371
Cdd:cd02665    92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVPY 164
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-377 4.37e-33

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: 128.69  E-value: 4.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNV-LENCRSHTEKRNIMFMQELQYLFALMMGSNRKFVDPSAALDl 215
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 216 lkgAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNvnsprNKSENPMVQLFYGTF--LTEGVREGKPFCNNETFGQYPLQ 293
Cdd:cd02668    80 ---ALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN-----PDLKNIVQDLFRGEYsyVTQCSKCGRESSLPSKFYELELQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 294 VNGYRNLDECLEGAMVEgdvELLPSD---HSVKYGQERWFTK------LPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQ 364
Cdd:cd02668   152 LKGHKTLEECIDEFLKE---EQLTGDnqyFCESCNSKTDATRrirlttLPPTLNFQLLRFVFDRKTGAKKKLNASISFPE 228

                         250
                  ....*....|...
gi 2184285241 365 IIYMDRYMYRSKE 377
Cdd:cd02668   229 ILDMGEYLAESDE 241
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
136-372 3.90e-31

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.94  E-value: 3.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 136 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSlpqNVLENCRSHTEkrnIMFMQELQYLF-ALMMGSNRKFVDPSAALD 214
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS---PLSEDSRYNKD---INLLCALRDLFkALQKNSKSSSVSPKMFKK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 215 LLKGAFRS-SEEQQQDVSEFTHKLLDWLEDAFqlavnVNSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET------- 286
Cdd:pfam00443  75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLS---CGEVSetfepfs 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 287 FGQYPLQVNGYRNLDECLEGAMVE-------GDVELLPSDHSVKYGQ---ERWFTKLPPVLTFELSRFEFNQSlgQPEKI 356
Cdd:pfam00443 147 DLSLPIPGDSAELKTASLQICFLQfskleelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKL 224

                         250
                  ....*....|....*.
gi 2184285241 357 HNKLEFPQIIYMDRYM 372
Cdd:pfam00443 225 NTEVEFPLELDLSRYL 240
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 137-377 1.69e-28

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: 114.12  E-value: 1.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsyslpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 216
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 kgafrsseeQQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTE----GVREGKPFCNNETFGQYPL 292
Cdd:cd02257    21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTivclECGHESVSTEPELFLSLPL 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 293 QVNG--YRNLDECLEGAMVEGDVELLPSDH-----SVKYGQERWFTKLPPVLTFELSRFEFNQSlGQPEKIHNKLEFPQI 365
Cdd:cd02257    92 PVKGlpQVSLEDCLEKFFKEEILEGDNCYKcekkkKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170

                         250
                  ....*....|..
gi 2184285241 366 IYMDRYMYRSKE 377
Cdd:cd02257   171 LDLSPYLSEGEK 182
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 136-372 2.73e-24

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 103.88  E-value: 2.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 136 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVlsYSLPQNVLEncrshTEKRNIMFmqELQYLFALMMGSNRKFVDPSAALDL 215
Cdd:cd02659     3 VGLKNQGATCYMNSLLQQLYMTPEFRNAV--YSIPPTEDD-----DDNKSVPL--ALQRLFLFLQLSESPVKTTELTDKT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 216 LKGAFRSSEE-QQQDVSEFTHKLLDWLEDAfqlavnvnSPRNKSENPMVQLFYGTFLTEGVREGkpfCNN-----ETFGQ 289
Cdd:cd02659    74 RSFGWDSLNTfEQHDVQEFFRVLFDKLEEK--------LKGTGQEGLIKNLFGGKLVNYIICKE---CPHesereEYFLD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 290 YPLQVNGYRNLDECLEgAMVEGdvELLPSD---HSVKYGQER------WFTKLPPVLTFELSRFEFNQSLGQPEKIHNKL 360
Cdd:cd02659   143 LQVAVKGKKNLEESLD-AYVQG--ETLEGDnkyFCEKCGKKVdaekgvCFKKLPPVLTLQLKRFEFDFETMMRIKINDRF 219

                         250
                  ....*....|..
gi 2184285241 361 EFPQIIYMDRYM 372
Cdd:cd02659   220 EFPLELDMEPYT 231
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 136-377 6.58e-14

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 74.91  E-value: 6.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241  136 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVlsYSLPQNvlencrsHTEKRNIMFMQeLQYLFALMMGSNrkfvDPSAALDL 215
Cdd:COG5077    194 VGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTD-------HPRGRDSVALA-LQRLFYNLQTGE----EPVDTTEL 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241  216 LKGAFRSSEEQ--QQDVSEFTHKLLDWLEDafqlavnvNSPRNKSENPMVQLFYGTFLT--EGVREGKPFCNNETFGQYP 291
Cdd:COG5077    260 TRSFGWDSDDSfmQHDIQEFNRVLQDNLEK--------SMRGTVVENALNGIFVGKMKSyiKCVNVNYESARVEDFWDIQ 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241  292 LQVNGYRNLDECLEGAMvegDVELLPSDHsvKYGQERW----------FTKLPPVLTFELSRFEFNQSLGQPEKIHNKLE 361
Cdd:COG5077    332 LNVKGMKNLQESFRRYI---QVETLDGDN--RYNAEKHglqdakkgviFESLPPVLHLQLKRFEYDFERDMMVKINDRYE 406

                          250       260
                   ....*....|....*....|
gi 2184285241  362 FPQII----YMDRYMYRSKE 377
Cdd:COG5077    407 FPLEIdllpFLDRDADKSEN 426
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 135-377 2.46e-13

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: 70.77  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 135 PVGLKNVGNTCWFSAVIQSLFQLPEFrrlvLSYSLPQNVLENCRSHtekrNIMFMQELQYLFALMMGSNRKFVDP---SA 211
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPL----ANYLLSREHSKDCCNE----GFCMMCALEAHVERALASSGPGSAPrifSS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 212 ALDLLKGAFRSSeeQQQDVSEFTHKLLDWLE----DAFQLAVNVNsPRNKSENPMVQLFyGTFLTEGVREGKpfCNNE-- 285
Cdd:cd02661    73 NLKQISKHFRIG--RQEDAHEFLRYLLDAMQkaclDRFKKLKAVD-PSSQETTLVQQIF-GGYLRSQVKCLN--CKHVsn 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 286 TFGQY---PLQVNGYRNLDECLEGAMvegDVELLpsDHSVKYGQER---------WFT--KLPPVLTFELSRFEFNQSlg 351
Cdd:cd02661   147 TYDPFldlSLDIKGADSLEDALEQFT---KPEQL--DGENKYKCERckkkvkaskQLTihRAPNVLTIHLKRFSNFRG-- 219

                         250       260
                  ....*....|....*....|....*.
gi 2184285241 352 qpEKIHNKLEFPQIIYMDRYMYRSKE 377
Cdd:cd02661   220 --GKINKQISFPETLDLSPYMSQPND 243
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-364 2.72e-13

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: 70.82  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSlpqnvleNCRSHTEKRNIMFMQELQYLFAlMMGSNRKFVDPSAALDLL 216
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYN-------PARRGANQSSDNLTNALRDLFD-TMDKKQEPVPPIEFLQLL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 KGAFRSSEEQ-------QQDVSEFTHKLLdwleDAFQLAVnvnsPRNKSENPMV-QLFYGTFLTEGVREGKPFCNNETFG 288
Cdd:cd02657    73 RMAFPQFAEKqnqggyaQQDAEECWSQLL----SVLSQKL----PGAGSKGSFIdQLFGIELETKMKCTESPDEEEVSTE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 289 Q-YPLQVN-----GYRNLDECLEGAMVEGDVELLPSDHS-VKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLE 361
Cdd:cd02657   145 SeYKLQCHisittEVNYLQDGLKKGLEEEIEKHSPTLGRdAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224


                  ...
gi 2184285241 362 FPQ 364
Cdd:cd02657   225 FPF 227
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 135-403 3.40e-12

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: 67.90  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 135 PVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSY---------SLPQNVLENCRSHT---EKRNIMFMQELQYLFALMMGS 202
Cdd:cd02666     1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFdeskaelasDYPTERRIGGREVSrseLQRSNQFVYELRSLFNDLIHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 203 NRKFVDPSAALDLLkgAFRsseeqQQDVSEFTHKLLDWLEDAFQLAVNVNSPRN----KSENPMV-QLFYGTFLTEGVRE 277
Cdd:cd02666    81 NTRSVTPSKELAYL--ALR-----QQDVTECIDNVLFQLEVALEPISNAFAGPDteddKEQSDLIkRLFSGKTKQQLVPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 278 GKPFCNN-----ETFGQypLQVNgyrNLDECLEGAMVEGDVELLpsDHSVKYGQERWFTKLPPVLtfelsrFEFNQSLGq 352
Cdd:cd02666   154 SMGNQPSvrtktERFLS--LLVD---VGKKGREIVVLLEPKDLY--DALDRYFDYDSLTKLPQRS------QVQAQLAQ- 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 353 pekihnkLEFPQIIYMDRYMYRS---------KELIRNKRECIRKLKEEIKILQQKLERY 403
Cdd:cd02666   220 -------PLQRELISMDRYELPSsiddideliREAIQSESSLVRQAQNELAELKHEIEKQ 272
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-376 2.81e-10

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: 62.00  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYslpqnvLENCRSHTEKRNIMFMQELQYLFALMMGSNRKfvDPSAALDLL 216
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSD------RHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--SPYGPINLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 KGAFRSSEE----QQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGkpfCNNET------ 286
Cdd:cd02660    74 YLSWKHSRNlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQR---CGGVSttvdpf 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 287 --------------FGQYPLQVNGYRNLDECLEGAMVEgdvELLPSD----HSVKYGQE--RWFT--KLPPVLTFELSRF 344
Cdd:cd02660   151 ldlsldipnkstpsWALGESGVSGTPTLSDCLDRFTRP---EKLGDFaykcSGCGSTQEatKQLSikKLPPVLCFQLKRF 227

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2184285241 345 EFNQSlGQPEKIHNKLEFPQIIYMDRYMYRSK 376
Cdd:cd02660   228 EHSLN-KTSRKIDTYVQFPLELNMTPYTSSSI 258
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-241 4.70e-10

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: 61.35  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNvlencrshTEKRNIMFMqeLQYLFALMMGSNRKfvdPSAALDLL 216
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--------GDSQSVMKK--LQLLQAHLMHTQRR---AEAPPDYF 67

                          90       100
                  ....*....|....*....|....*...
gi 2184285241 217 KGAFRS---SEEQQQDVSEFTHKLLDWL 241
Cdd:cd02664    68 LEASRPpwfTPGSQQDCSEYLRYLLDRL 95
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
137-361 6.96e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 60.20  E-value: 6.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSL-FQLPEFRRLVLSYSLPQNVLENcrSHTEKRNIMFMQELQYLFALMMGSNRkfvdpsaaldl 215
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKN--VIRKPEPDLNQEEALKLFTALWSSKE----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 216 LKGAFRSSEEQQQDVSEFTHKLLDWLedafqlavnvNSPRNKSenpmVQLFYGTFLTEGVREG-KPFCNNETFGQYPLQV 294
Cdd:COG5533    68 HKVGWIPPMGSQEDAHELLGKLLDEL----------KLDLVNS----FTIRIFKTTKDKKKTStGDWFDIIIELPDQTWV 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2184285241 295 NGYRNLDECLEGAMVEGDVELL------PSDHSV-KYGQERWFTKLPPVLTFELSRFEFNqslGQPEKIHNKLE 361
Cdd:COG5533   134 NNLKTLQEFIDNMEELVDDETGvkakenEELEVQaKQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD 204
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-372 3.24e-09

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: 58.17  E-value: 3.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEFRRLVLsyslpqnvlencrshtEKRNIMFMQelqylfalmmgsnrkfvdpsaaldLL 216
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLS----------------ETPKELFSQ------------------------VC 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 KGAFRSSEEQQQDVSEFTHKLLDWLedafqlavnvnsprnkseNPMVQLFYGTFLT-----EGVREGKpfCNNETFGQYP 291
Cdd:cd02667    41 RKAPQFKGYQQQDSHELLRYLLDGL------------------RTFIDSIFGGELTstimcESCGTVS--LVYEPFLDLS 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 292 LQV----NGYRNLDECL----EGAMVEGDVELLpSDHSVKYGQERWFTKLPPVLTFELSRFeFNQSLGQPEKIHNKLEFP 363
Cdd:cd02667   101 LPRsdeiKSECSIESCLkqftEVEILEGNNKFA-CENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSFP 178


                  ....*....
gi 2184285241 364 QIIYMDRYM 372
Cdd:cd02667   179 EILDLAPFC 187
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-364 2.01e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 52.70  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsyslpqNVLENCrshtekrnimfmqeLQYLFALMMGSNRKF--VDPSAALD 214
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYF---------------ENLLTC--------------LKDLFESISEQKKRTgvISPKKFIT 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 215 LLK---GAFRSSeeQQQDVSEFTHKLL----DWLEDAFQLAVNVNSPRNKSENPMV-----QLFYGTFLTEgVRegkpfC 282
Cdd:cd02663    52 RLKrenELFDNY--MHQDAHEFLNFLLneiaEILDAERKAEKANRKLNNNNNAEPQptwvhEIFQGILTNE-TR-----C 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 283 --------NNETFGQYPLQVNGYRNLDECLEGAMVEgdvELLPSDH--------SVKYGQERW-FTKLPPVLTFELSRFE 345
Cdd:cd02663   124 ltcetvssRDETFLDLSIDVEQNTSITSCLRQFSAT---ETLCGRNkfycdeccSLQEAEKRMkIKKLPKILALHLKRFK 200

                         250
                  ....*....|....*....
gi 2184285241 346 FNQSLGQPEKIHNKLEFPQ 364
Cdd:cd02663   201 YDEQLNRYIKLFYRVVFPL 219
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-371 1.22e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 44.24  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQLPEF-RRLVLSYSLPQNVLENCRSHTEkrnimfMQELQYLFALMMGSNRK-FVDPSAALD 214
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDLN------CQLIKLADGLLSGRYSKpASLKSENDP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 215 LLKG----AFRS---------SEEQQQDVSEFTHKLLDWLEDafqlavnvNSPRNKSENP--MVQLFYGTFL----TEGV 275
Cdd:cd02658    75 YQVGikpsMFKAligkghpefSTMRQQDALEFLLHLIDKLDR--------ESFKNLGLNPndLFKFMIEDRLeclsCKKV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 276 REGKPFCNN---------ETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYG--QERWFTKLPPVLTFELSRF 344
Cdd:cd02658   147 KYTSELSEIlslpvpkdeATEKEEGELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTTatKTTGFKTFPDYLVINMKRF 226

                         250       260
                  ....*....|....*....|....*..
gi 2184285241 345 EFNQSlGQPEKIHNKLEFPQIIYMDRY 371
Cdd:cd02658   227 QLLEN-WVPKKLDVPIDVPEELGPGKY 252
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 137-363 8.61e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 41.12  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 137 GLKNVGNTCWFSAVIQSLFQlpefrrlvlsyslpqnvlencrshtekrnimfmqelqylfalmmgsnrkfvdpsaaldll 216
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 217 kgafrsseeQQQDVSEFTHKLLDWLEDAfqlavnvnsprnksenpMVQLFYGTFL--TEGVREGKPFCNNETFgqYPLQV 294
Cdd:cd02674    21 ---------DQQDAQEFLLFLLDGLHSI-----------------IVDLFQGQLKsrLTCLTCGKTSTTFEPF--TYLSL 72

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 295 N--------GYRNLDECLEGAMVEgdvELLPSD---HSVKYGQERWFTK------LPPVLTFELSRFEFNQslGQPEKIH 357
Cdd:cd02674    73 PipsgsgdaPKVTLEDCLRLFTKE---ETLDGDnawKCPKCKKKRKATKkltisrLPKVLIIHLKRFSFSR--GSTRKLT 147


                  ....*.
gi 2184285241 358 NKLEFP 363
Cdd:cd02674   148 TPVTFP 153
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 136-394 6.05e-03

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 39.22  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 136 VGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNVLENCrSHTEKRNIMFMQEL-------------QYLFALMMGS 202
Cdd:cd02669   120 VGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRK-SELVKRLSELIRKIwnprnfkghvsphELLQAVSKVS 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 203 NRKFvdpsaaldllkgafrsSEEQQQDVSEF-------THKLLDW--------LEDAFQLAVNVNS---PRNKSENPMVQ 264
Cdd:cd02669   199 KKKF----------------SITEQSDPVEFlswllntLHKDLGGskkpnssiIHDCFQGKVQIETqkiKPHAEEEGSKD 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184285241 265 LFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYR-------NLDECLEGamVEGDVELLPSDHSVKYGQerwfTKLPPVL 337
Cdd:cd02669   263 KFFKDSRVKKTSVSPFLLLTLDLPPPPLFKDGNEeniipqvPLKQLLKK--YDGKTETELKDSLKRYLI----SRLPKYL 336

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2184285241 338 TFELSRFEFNQslGQPEKihNK--LEFPQIIyMDRYMYRSKELIRNKRECIRKLKEEIK 394
Cdd:cd02669   337 IFHIKRFSKNN--FFKEK--NPtiVNFPIKN-LDLSDYVHFDKPSLNLSTKYNLVANIV 390
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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