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Conserved domains on  [gi|1907069350|ref|XP_036021582|]
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ubiquitin carboxyl-terminal hydrolase 37 isoform X1 [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12179965)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the-terminal Gly of ubiquitin, a 76-residue protein attached to proteins as an intracellular targeting signal

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
342-601 2.61e-54

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 191.50  E-value: 2.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFAnDLLKQSIPWKKI----PFNALIRRFANLlIKKDICNSETKKELLKKVKNAISAT 417
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDsrynKDINLLCALRDL-FKALQKNSKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 418 AERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVlgeenlpdtsaTKVFTcpvitnleFEVQHSIICKACGETIP 497
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLI-----------TDLFR--------GQLKSRLKCLSCGEVSE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 498 KREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELE----YSCEKCGGKC-ALVRHKFNRLPRVLILHLKRYSFNVal 572
Cdd:pfam00443 141 TFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDdeekYYCDKCGCKQdAIKQLKISRLPPVLIIHLKRFSYNR-- 218
                         250       260
                  ....*....|....*....|....*....
gi 1907069350 573 SLNNKLGQQVIIPRFLTLASHCTESTKPP 601
Cdd:pfam00443 219 STWEKLNTEVEFPLELDLSRYLAEELKPK 247
UCH_N pfam16674
N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the ...
3-105 2.16e-52

N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the N-terminus of ubiquitin carboxyl-terminal hydrolase 37 or 26. The function is not known.


:

Pssm-ID: 465227  Cd Length: 102  Bit Score: 178.19  E-value: 2.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350   3 PLKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGiPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFL 82
Cdd:pfam16674   1 PLKVHGFVQIWSKKTGMSKWKEAFIEIVEKKKKVKLVVYFNTGG-PKTFQLNNNIKSVVLRSYGEKQNRLHLTLKNNSFL 79
                          90       100
                  ....*....|....*....|...
gi 1907069350  83 SIDKVPSKDAEEMRLFLDAVHQN 105
Cdd:pfam16674  80 FIDKLSSTDAEELKMFLDRVHQN 102
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
886-949 5.11e-15

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: 75.98  E-value: 5.11e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069350 886 PHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRS--GYIFFYM 949
Cdd:cd02257   190 SYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSssAYILFYE 255
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
342-601 2.61e-54

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 191.50  E-value: 2.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFAnDLLKQSIPWKKI----PFNALIRRFANLlIKKDICNSETKKELLKKVKNAISAT 417
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDsrynKDINLLCALRDL-FKALQKNSKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 418 AERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVlgeenlpdtsaTKVFTcpvitnleFEVQHSIICKACGETIP 497
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLI-----------TDLFR--------GQLKSRLKCLSCGEVSE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 498 KREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELE----YSCEKCGGKC-ALVRHKFNRLPRVLILHLKRYSFNVal 572
Cdd:pfam00443 141 TFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDdeekYYCDKCGCKQdAIKQLKISRLPPVLIIHLKRFSYNR-- 218
                         250       260
                  ....*....|....*....|....*....
gi 1907069350 573 SLNNKLGQQVIIPRFLTLASHCTESTKPP 601
Cdd:pfam00443 219 STWEKLNTEVEFPLELDLSRYLAEELKPK 247
UCH_N pfam16674
N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the ...
3-105 2.16e-52

N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the N-terminus of ubiquitin carboxyl-terminal hydrolase 37 or 26. The function is not known.


Pssm-ID: 465227  Cd Length: 102  Bit Score: 178.19  E-value: 2.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350   3 PLKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGiPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFL 82
Cdd:pfam16674   1 PLKVHGFVQIWSKKTGMSKWKEAFIEIVEKKKKVKLVVYFNTGG-PKTFQLNNNIKSVVLRSYGEKQNRLHLTLKNNSFL 79
                          90       100
                  ....*....|....*....|...
gi 1907069350  83 SIDKVPSKDAEEMRLFLDAVHQN 105
Cdd:pfam16674  80 FIDKLSSTDAEELKMFLDRVHQN 102
PH_USP37_like cd13312
Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37; Members here ...
4-106 5.17e-51

Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37; Members here include USP37, USP29, and USP26. All of these contain a single PH-like domain. USP37 (also called ubiquitin carboxyl-terminal hydrolase 37, ubiquitin thiolesterase 37, deubiquitinating enzyme 37, and tmp_locus_50) is a deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry. USP37 mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex and 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). USP29 (also called ubiquitin carboxyl-terminal hydrolase 29, ubiquitin thiolesterase 29, deubiquitinating enzyme 29, and HOM-TES-84/86) plays a role in apoptosis and oxidative stress. In response to oxidative stress, JTV1 dissociates from the ARS complex, translocates to the nucleus, associates with far upstream element binding protein (FBP) and co-activates the transcription of USP29 which binds to, cleaves poly-ubiquitin chains from, and stabilizes p53 leading to apoptosis. The X-linked deubiquitination enzyme USP26 (also called ubiquitin carboxyl-terminal hydrolase 26, ubiquitin thiolesterase 26, and deubiquitinating enzyme 26) is a regulator of androgen receptor (AR) signaling. It binds to AR using three nuclear receptor interaction motifs (LXXLL, FXXLF and FXXFF) and modulates AR ubiquitination. Polymorphism of Usp26 correlates with idiopathic male infertility. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270122  Cd Length: 103  Bit Score: 174.42  E-value: 5.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350   4 LKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGIPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFLS 83
Cdd:cd13312     1 LKIHGFVQIWSKKTGMTKWKEAFIEIVEGKKKVKLVVYFKTGGKPKTFQLSNNIKSVVLRSYGGNQNHLHLTLKNNSFLF 80
                          90       100
                  ....*....|....*....|...
gi 1907069350  84 IDKVPSKDAEEMRLFLDAVHQNR 106
Cdd:cd13312    81 IDKLSSTDAEQLKEFLDKVHQKK 103
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
342-601 1.60e-34

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: 132.99  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSlqsfandllkqsipwkkipfnalirrfanllikkdicnsetkkellkkvknaisataerf 421
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 422 sgyVQNDAHEFLSQCLDQLKEDMEKLNKtwktepvlgeenlpDTSATKVFTCPVITNLEFEVQHSIICKACGETIPKREQ 501
Cdd:cd02257    21 ---EQQDAHEFLLFLLDKLHEELKKSSK--------------RTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEP 83
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 502 FNDLSIDLPrrKKPLPPRSIQDSLDLFFRAEELE----YSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSlNNK 577
Cdd:cd02257    84 ELFLSLPLP--VKGLPQVSLEDCLEKFFKEEILEgdncYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGT-KEK 160
                         250       260
                  ....*....|....*....|....
gi 1907069350 578 LGQQVIIPRFLTLASHCTESTKPP 601
Cdd:cd02257   161 LNTKVSFPLELDLSPYLSEGEKDS 184
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
886-949 5.11e-15

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: 75.98  E-value: 5.11e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069350 886 PHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRS--GYIFFYM 949
Cdd:cd02257   190 SYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSssAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
865-948 2.32e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 69.01  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 865 DM-EYTEAEAEELKRNAEtgalphSYRLISVVSHIGStSSSGHYISDVYDIKKQAWFTYNDLEVSKI-QEAAVQSDrdrS 942
Cdd:pfam00443 235 DLsRYLAEELKPKTNNLQ------DYRLVAVVVHSGS-LSSGHYIAYIKAYENNRWYKFDDEKVTEVdEETAVLSS---S 304

                  ....*.
gi 1907069350 943 GYIFFY 948
Cdd:pfam00443 305 AYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
342-514 2.00e-11

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 67.99  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQS----FANDLLKQSIPWK--KIPFNALIRRFANLLikKDICNSETKKELLKKVKNAIS 415
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWElrdyFLSDEYEESINEEnpLGMHGSVASAYADLI--KQLYDGNLHAFTPSGFKKTIG 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 416 ATAERFSGYVQNDAHEFLSQCLDQLKEDMEKL-NKTWKTEPVLGEENLPDTSAT--------KVFTCPVITNL-EFEVQH 485
Cdd:COG5560   345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIiKKPYTSKPDLSPGDDVVVKKKakecwwehLKRNDSIITDLfQGMYKS 424
                         170       180
                  ....*....|....*....|....*....
gi 1907069350 486 SIICKACGETIPKREQFNDLSIDLPRRKK 514
Cdd:COG5560   425 TLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
887-948 5.32e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 52.50  E-value: 5.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069350 887 HSYRLISVVSHIGSTSSsGHYISDVYdiKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFY 948
Cdd:COG5533   223 TYYDLVGFVLHQGSLEG-GHYIAYVK--KGGKWEKANDSDVTPVSEEEAINEKAKNAYLYFY 281
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
342-601 2.61e-54

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 191.50  E-value: 2.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFAnDLLKQSIPWKKI----PFNALIRRFANLlIKKDICNSETKKELLKKVKNAISAT 417
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDsrynKDINLLCALRDL-FKALQKNSKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 418 AERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVlgeenlpdtsaTKVFTcpvitnleFEVQHSIICKACGETIP 497
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLI-----------TDLFR--------GQLKSRLKCLSCGEVSE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 498 KREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELE----YSCEKCGGKC-ALVRHKFNRLPRVLILHLKRYSFNVal 572
Cdd:pfam00443 141 TFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDdeekYYCDKCGCKQdAIKQLKISRLPPVLIIHLKRFSYNR-- 218
                         250       260
                  ....*....|....*....|....*....
gi 1907069350 573 SLNNKLGQQVIIPRFLTLASHCTESTKPP 601
Cdd:pfam00443 219 STWEKLNTEVEFPLELDLSRYLAEELKPK 247
UCH_N pfam16674
N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the ...
3-105 2.16e-52

N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the N-terminus of ubiquitin carboxyl-terminal hydrolase 37 or 26. The function is not known.


Pssm-ID: 465227  Cd Length: 102  Bit Score: 178.19  E-value: 2.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350   3 PLKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGiPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFL 82
Cdd:pfam16674   1 PLKVHGFVQIWSKKTGMSKWKEAFIEIVEKKKKVKLVVYFNTGG-PKTFQLNNNIKSVVLRSYGEKQNRLHLTLKNNSFL 79
                          90       100
                  ....*....|....*....|...
gi 1907069350  83 SIDKVPSKDAEEMRLFLDAVHQN 105
Cdd:pfam16674  80 FIDKLSSTDAEELKMFLDRVHQN 102
PH_USP37_like cd13312
Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37; Members here ...
4-106 5.17e-51

Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37; Members here include USP37, USP29, and USP26. All of these contain a single PH-like domain. USP37 (also called ubiquitin carboxyl-terminal hydrolase 37, ubiquitin thiolesterase 37, deubiquitinating enzyme 37, and tmp_locus_50) is a deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry. USP37 mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex and 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). USP29 (also called ubiquitin carboxyl-terminal hydrolase 29, ubiquitin thiolesterase 29, deubiquitinating enzyme 29, and HOM-TES-84/86) plays a role in apoptosis and oxidative stress. In response to oxidative stress, JTV1 dissociates from the ARS complex, translocates to the nucleus, associates with far upstream element binding protein (FBP) and co-activates the transcription of USP29 which binds to, cleaves poly-ubiquitin chains from, and stabilizes p53 leading to apoptosis. The X-linked deubiquitination enzyme USP26 (also called ubiquitin carboxyl-terminal hydrolase 26, ubiquitin thiolesterase 26, and deubiquitinating enzyme 26) is a regulator of androgen receptor (AR) signaling. It binds to AR using three nuclear receptor interaction motifs (LXXLL, FXXLF and FXXFF) and modulates AR ubiquitination. Polymorphism of Usp26 correlates with idiopathic male infertility. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270122  Cd Length: 103  Bit Score: 174.42  E-value: 5.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350   4 LKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGIPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFLS 83
Cdd:cd13312     1 LKIHGFVQIWSKKTGMTKWKEAFIEIVEGKKKVKLVVYFKTGGKPKTFQLSNNIKSVVLRSYGGNQNHLHLTLKNNSFLF 80
                          90       100
                  ....*....|....*....|...
gi 1907069350  84 IDKVPSKDAEEMRLFLDAVHQNR 106
Cdd:cd13312    81 IDKLSSTDAEQLKEFLDKVHQKK 103
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
342-601 1.60e-34

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: 132.99  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSlqsfandllkqsipwkkipfnalirrfanllikkdicnsetkkellkkvknaisataerf 421
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 422 sgyVQNDAHEFLSQCLDQLKEDMEKLNKtwktepvlgeenlpDTSATKVFTCPVITNLEFEVQHSIICKACGETIPKREQ 501
Cdd:cd02257    21 ---EQQDAHEFLLFLLDKLHEELKKSSK--------------RTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEP 83
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 502 FNDLSIDLPrrKKPLPPRSIQDSLDLFFRAEELE----YSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSlNNK 577
Cdd:cd02257    84 ELFLSLPLP--VKGLPQVSLEDCLEKFFKEEILEgdncYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGT-KEK 160
                         250       260
                  ....*....|....*....|....
gi 1907069350 578 LGQQVIIPRFLTLASHCTESTKPP 601
Cdd:cd02257   161 LNTKVSFPLELDLSPYLSEGEKDS 184
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-601 6.81e-27

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: 112.74  E-value: 6.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFANDLL-----KQSIPWKKIPfNAL--IRRFANLLIKKDICNSETKKelLKKVKNAI 414
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYsipptEDDDDNKSVP-LALqrLFLFLQLSESPVKTTELTDK--TRSFGWDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 415 SATaerfsgYVQNDAHEFLSQCLDQLKEDMEKlnktwktepvLGEENLpdtsatkvftcpvITNLeFEVQHS--IICKAC 492
Cdd:cd02659    81 LNT------FEQHDVQEFFRVLFDKLEEKLKG----------TGQEGL-------------IKNL-FGGKLVnyIICKEC 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 493 GETIPKREQFNDLSIDLprrkkpLPPRSIQDSLDLFFRAEELE----YSCEKCGGKC-ALVRHKFNRLPRVLILHLKRYS 567
Cdd:cd02659   131 PHESEREEYFLDLQVAV------KGKKNLEESLDAYVQGETLEgdnkYFCEKCGKKVdAEKGVCFKKLPPVLTLQLKRFE 204
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907069350 568 FNVALSLNNKLGQQVIIPRFLTLASHCTESTKPP 601
Cdd:cd02659   205 FDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-600 1.99e-25

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: 107.78  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFslqsfandllkqsipwkkipfnalirrFANLLIK-KDI--CNSETKKEL----LKKVKNAI 414
Cdd:cd02663     1 GLENFGNTCYCNSVLQALY---------------------------FENLLTClKDLfeSISEQKKRTgvisPKKFITRL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 415 SATAERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVLGEENLPDTSATKVFTC--PVITNlefevqhSIICKAC 492
Cdd:cd02663    54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIfqGILTN-------ETRCLTC 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 493 gETIPKR-EQFNDLSIDLPrrkkplPPRSIQDSLDLFFRAEEL----EYSCEKCGGKC-ALVRHKFNRLPRVLILHLKRY 566
Cdd:cd02663   127 -ETVSSRdETFLDLSIDVE------QNTSITSCLRQFSATETLcgrnKFYCDECCSLQeAEKRMKIKKLPKILALHLKRF 199
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907069350 567 SFNVALSLNNKLGQQVIIPRFLTLASHCTESTKP 600
Cdd:cd02663   200 KYDEQLNRYIKLFYRVVFPLELRLFNTTDDAENP 233
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-588 2.39e-22

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 98.93  E-value: 2.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFA----NDLLKQSIPWKKIP--FNALIRRFANLLIKKDICNSETKKELLKK------ 409
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQwrydDLENKFPSDVVDPAndLNCQLIKLADGLLSGRYSKPASLKSENDPyqvgik 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 410 ---VKNAISATAERFSGYVQNDAHEFLSQCLDQLKedmEKLNKTWKTEPvlgeenlpdtsatkvftcpvITNLEFEVQHS 486
Cdd:cd02658    81 psmFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD---RESFKNLGLNP--------------------NDLFKFMIEDR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 487 IICKACGETIPKREQFNDLSIDLPRR--------KKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKC-ALVRHKFNRLPR 557
Cdd:cd02658   138 LECLSCKKVKYTSELSEILSLPVPKDeatekeegELVYEPVPLEDCLKAYFAPETIEDFCSTCKEKTtATKTTGFKTFPD 217
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907069350 558 VLILHLKRYSFN---VALSLNNklgqQVIIPRFL 588
Cdd:cd02658   218 YLVINMKRFQLLenwVPKKLDV----PIDVPEEL 247
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-595 8.84e-22

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 96.30  E-value: 8.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLqsfandllkqsipwkkipfNALIRRFanllikkdicnSETKKELLKKVknaiSATAERF 421
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQT-------------------PALRELL-----------SETPKELFSQV----CRKAPQF 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 422 SGYVQNDAHEFLSQCLDQLkedmeklnktwktepvlgeENLPDtsatKVFTCpvitnlefEVQHSIICKACGETIPKREQ 501
Cdd:cd02667    47 KGYQQQDSHELLRYLLDGL-------------------RTFID----SIFGG--------ELTSTIMCESCGTVSLVYEP 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 502 FNDLSidLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKC--ALVRHKFNRLPRVLILHLKRYSFNVALSLnNKLG 579
Cdd:cd02667    96 FLDLS--LPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCtkAKKQYLISKLPPVLVIHLKRFQQPRSANL-RKVS 172
                         250
                  ....*....|....*.
gi 1907069350 580 QQVIIPRFLTLASHCT 595
Cdd:cd02667   173 RHVSFPEILDLAPFCD 188
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
341-599 3.43e-21

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 95.90  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 341 QGFSNLGNTCYMNAILQSLFSLQSFANDLLKQ---SIPWKKIPFN----ALIRRFANLLIKKDIcNSETKKELLKKVKNA 413
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDrhsCTCLSCSPNSclscAMDEIFQEFYYSGDR-SPYGPINLLYLSWKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 414 isatAERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPvlgeenlpdtsatkvfTCPVITNLEFE--VQHSIICKA 491
Cdd:cd02660    80 ----SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDES----------------HCNCIIHQTFSgsLQSSVTCQR 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 492 CGETIPKREQFNDLSIDLPRRKKPLPPRS---------IQDSLDLFFRAEELE---YSCEKCGGKCALVRH-KFNRLPRV 558
Cdd:cd02660   140 CGGVSTTVDPFLDLSLDIPNKSTPSWALGesgvsgtptLSDCLDRFTRPEKLGdfaYKCSGCGSTQEATKQlSIKKLPPV 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907069350 559 LILHLKRYSFNvALSLNNKLGQQVIIPRFLTLASHCTESTK 599
Cdd:cd02660   220 LCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSSIG 259
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-604 3.64e-21

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 93.51  E-value: 3.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLfslqsfANDllkqsipwkkipfnalirrfanllikkdicnsetkkellkkvknaisataerf 421
Cdd:cd02674     1 GLRNLGNTCYMNSILQCL------SAD----------------------------------------------------- 21
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 422 sgyvQNDAHEFLSQCLDQLKEdmeklnktwktepvlgeenlpdtsatkvftcpVITNLeFEVQH--SIICKACGETIPKR 499
Cdd:cd02674    22 ----QQDAQEFLLFLLDGLHS--------------------------------IIVDL-FQGQLksRLTCLTCGKTSTTF 64
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 500 EQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELE----YSCEKCGGK-CALVRHKFNRLPRVLILHLKRYSFNVALSl 574
Cdd:cd02674    65 EPFTYLSLPIPSGSGDAPKVTLEDCLRLFTKEETLDgdnaWKCPKCKKKrKATKKLTISRLPKVLIIHLKRFSFSRGST- 143
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907069350 575 nNKLGQQVIIP-RFLTLASHCTESTKPPVTL 604
Cdd:cd02674   144 -RKLTTPVTFPlNDLDLTPYVDTRSFTGPFK 173
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-603 1.29e-20

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: 93.49  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFANDLL----KQSIPWKKIPFNALIRRFANLLIKKDICNSETkkellKKVKNAISAT 417
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLsrehSKDCCNEGFCMMCALEAHVERALASSGPGSAP-----RIFSSNLKQI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 418 AERFSGYVQNDAHEFLSQCLDQL-KEDMEKLNKTWKTEPVLGEENLpdtsatkvftcpvitnlefeVQH--------SII 488
Cdd:cd02661    78 SKHFRIGRQEDAHEFLRYLLDAMqKACLDRFKKLKAVDPSSQETTL--------------------VQQifggylrsQVK 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 489 CKACGETIPKREQFNDLSIDLPRRKkplpprSIQDSLDLFFRAEELE----YSCEKCGGKC-ALVRHKFNRLPRVLILHL 563
Cdd:cd02661   138 CLNCKHVSNTYDPFLDLSLDIKGAD------SLEDALEQFTKPEQLDgenkYKCERCKKKVkASKQLTIHRAPNVLTIHL 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907069350 564 KRYSFNVAlslnNKLGQQVIIPRFLTLASHCTESTKPPVT 603
Cdd:cd02661   212 KRFSNFRG----GKINKQISFPETLDLSPYMSQPNDGPLK 247
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-590 4.22e-18

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: 86.78  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFANDLLKQSIPWKK---IPFNALIRRFANLLIKKDICNSETKKELLkkvknaiSATA 418
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGdsqSVMKKLQLLQAHLMHTQRRAEAPPDYFLE-------ASRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 419 ERFSGYVQNDAHEFLSQCLDQLkedmeklnktwktepvlgeenlpDTSATKVFTCPVITNlefevqhsIICKACGETIPK 498
Cdd:cd02664    74 PWFTPGSQQDCSEYLRYLLDRL-----------------------HTLIEKMFGGKLSTT--------IRCLNCNSTSAR 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 499 REQFNDLSIDLPrrkkplpprSIQDSLDLFFRAEEL----EYSCEKCGGKCALVRH-KFNRLPRVLILHLKRYSFNVALS 573
Cdd:cd02664   123 TERFRDLDLSFP---------SVQDLLNYFLSPEKLtgdnQYYCEKCASLQDAEKEmKVTGAPEYLILTLLRFSYDQKTH 193
                         250
                  ....*....|....*..
gi 1907069350 574 LNNKLGQQVIIPRFLTL 590
Cdd:cd02664   194 VREKIMDNVSINEVLSL 210
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-569 2.62e-15

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: 78.40  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFANDL--LKQSIpwkkipfNALIRRFANLLIKKDICNSETKKELLKKVKNAISATAE 419
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLkhLVSLI-------SSVEQLQSSFLLNPEKYNDELANQAPRRLLNALREVNP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 420 RFSGYVQNDAHEFLSQCLDQLKEDMEKLnktWKTEPVLgeenlpdtsATKVFTCPVITNlefevqhsiickacgetipKR 499
Cdd:cd02671    99 MYEGYLQHDAQEVLQCILGNIQELVEKD---FQGQLVL---------RTRCLECETFTE-------------------RR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 500 EQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEEL-----------------EYSCEKCGGKCALVRH-KFNRLPRVLIL 561
Cdd:cd02671   148 EDFQDISVPVQESELSKSEESSEISPDPKTEMKTLkwaisqfasverivgedKYFCENCHHYTEAERSlLFDKLPEVITI 227

                  ....*...
gi 1907069350 562 HLKRYSFN 569
Cdd:cd02671   228 HLKCFAAN 235
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
886-949 5.11e-15

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: 75.98  E-value: 5.11e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069350 886 PHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRS--GYIFFYM 949
Cdd:cd02257   190 SYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSLSssAYILFYE 255
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-569 4.60e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 70.09  E-value: 4.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFAndllkqsipwkkipfnalirrfanllikkdicnsetkkELLKKVKNaisataerf 421
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLI--------------------------------------EYLEEFLE--------- 33
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 422 sgyvQNDAHEFLSQCLDQLkedmeklnktwktepvlgeENLPDTSatkvftcpvitnLEFEVQHSIICKACGE-TIPKRE 500
Cdd:cd02662    34 ----QQDAHELFQVLLETL-------------------EQLLKFP------------FDGLLASRIVCLQCGEsSKVRYE 78
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069350 501 QFNDLSIdlprrkkPLPPRSIQDSLDL------FFRAEELE-YSCEKCggkcalvRHKFNRLPRVLILHLKRYSFN 569
Cdd:cd02662    79 SFTMLSL-------PVPNQSSGSGTTLehclddFLSTEIIDdYKCDRC-------QTVIVRLPQILCIHLSRSVFD 140
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
865-948 2.32e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 69.01  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 865 DM-EYTEAEAEELKRNAEtgalphSYRLISVVSHIGStSSSGHYISDVYDIKKQAWFTYNDLEVSKI-QEAAVQSDrdrS 942
Cdd:pfam00443 235 DLsRYLAEELKPKTNNLQ------DYRLVAVVVHSGS-LSSGHYIAYIKAYENNRWYKFDDEKVTEVdEETAVLSS---S 304

                  ....*.
gi 1907069350 943 GYIFFY 948
Cdd:pfam00443 305 AYILFY 310
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-597 2.83e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 68.99  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFANDLLK----QSIPWKKIPFNA----------LIRRFANLLikkdicNSEtkkell 407
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstEDAELKNMPPDKphepqtiidqLQLIFAQLQ------FGN------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 408 KKVKNAIS-ATAERFSGYVQNDAHEFLSQCLDQLKEDMEK-LNKTWKTepvlgeenlpdtsatkvftcpVITNL-EFEVQ 484
Cdd:cd02668    69 RSVVDPSGfVKALGLDTGQQQDAQEFSKLFLSLLEAKLSKsKNPDLKN---------------------IVQDLfRGEYS 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 485 HSIICKACGETIPKREQFNDLSIDLPRRKKplpprsIQDSLDLFFRAEELE----YSCEKCGGKC-ALVRHKFNRLPRVL 559
Cdd:cd02668   128 YVTQCSKCGRESSLPSKFYELELQLKGHKT------LEECIDEFLKEEQLTgdnqYFCESCNSKTdATRRIRLTTLPPTL 201
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907069350 560 ILHLKRYSFNVALSLNNKLGQQVIIPRFLTLASHCTES 597
Cdd:cd02668   202 NFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAES 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
342-514 2.00e-11

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 67.99  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQS----FANDLLKQSIPWK--KIPFNALIRRFANLLikKDICNSETKKELLKKVKNAIS 415
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWElrdyFLSDEYEESINEEnpLGMHGSVASAYADLI--KQLYDGNLHAFTPSGFKKTIG 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 416 ATAERFSGYVQNDAHEFLSQCLDQLKEDMEKL-NKTWKTEPVLGEENLPDTSAT--------KVFTCPVITNL-EFEVQH 485
Cdd:COG5560   345 SFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIiKKPYTSKPDLSPGDDVVVKKKakecwwehLKRNDSIITDLfQGMYKS 424
                         170       180
                  ....*....|....*....|....*....
gi 1907069350 486 SIICKACGETIPKREQFNDLSIDLPRRKK 514
Cdd:COG5560   425 TLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
886-948 4.15e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 63.85  E-value: 4.15e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069350 886 PHSYRLISVVSHIGSTSSsGHYISDVYDIKKQAWFTYNDLEVSKIQEaavQSDRDRSGYIFFY 948
Cdd:cd02674   171 PFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDDSRVTKVSE---SSVVSSSAYILFY 229
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-569 8.32e-11

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 65.42  E-value: 8.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFAND-LLKQSIPWKKIPFNALIRRFAnLLIKKdICNSETKK------ELLKKVKNAi 414
Cdd:cd02669   121 GLNNIKNNDYANVIIQALSHVKPIRNFfLLYENYENIKDRKSELVKRLS-ELIRK-IWNPRNFKghvsphELLQAVSKV- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 415 saTAERFSGYVQNDAHEFLSQCLDQLKEDMEKLNK--------------TWKTEPVLGEENlPDTSATKVFTCpvitnle 480
Cdd:cd02669   198 --SKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKpnssiihdcfqgkvQIETQKIKPHAE-EEGSKDKFFKD------- 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 481 fEVQHSIIckacgeTIPkreqFNDLSIDLP--------RRKKPLPPRSIQDSLDLFFRAEELEYscekcggKCALVRHKF 552
Cdd:cd02669   268 -SRVKKTS------VSP----FLLLTLDLPppplfkdgNEENIIPQVPLKQLLKKYDGKTETEL-------KDSLKRYLI 329
                         250
                  ....*....|....*..
gi 1907069350 553 NRLPRVLILHLKRYSFN 569
Cdd:cd02669   330 SRLPKYLIFHIKRFSKN 346
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
345-593 2.62e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 58.69  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 345 NLGNTCYMNAILQSLFSLqsfandllkqsipwkkipfNALIRRFANLLikkdicnsetkkellkkvknaisataerfsgy 424
Cdd:cd02673     4 NTGNSCYFNSTMQALSSI-------------------GKINTEFDNDD-------------------------------- 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 425 vQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVLGEENLPdtsatkvftcpvITNLEFEVQHSIICKACGetipKREQFND 504
Cdd:cd02673    33 -QQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNP------------LEAFKYTIESSYVCIGCS----FEENVSD 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 505 LSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKLGQQVII 584
Cdd:cd02673    96 VGNFLDVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEIMK 175

                  ....*....
gi 1907069350 585 PRFLTLASH 593
Cdd:cd02673   176 KYCGTDAKY 184
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
342-569 3.47e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 57.57  E-value: 3.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350  342 GFSNLGNTCYMNAILQSLFSLQSFANDLLKqsIPWK------KIPFnALIRRFANLLiKKDICNSETkkELlkkVKNAIS 415
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYG--IPTDhprgrdSVAL-ALQRLFYNLQ-TGEEPVDTT--EL---TRSFGW 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350  416 ATAERFsgyVQNDAHEFLSQCLDQLKEDMeklnktwKTEPVlgEENLPDTSATKVFTCPVITNLEFEVQHSiickacget 495
Cdd:COG5077    266 DSDDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVV--ENALNGIFVGKMKSYIKCVNVNYESARV--------- 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350  496 ipkrEQFNDLSIDLPRRKkplpprSIQDSLDLFFRAEELE----YSCEKCGGKCAlvrHK---FNRLPRVLILHLKRYSF 568
Cdd:COG5077    325 ----EDFWDIQLNVKGMK------NLQESFRRYIQVETLDgdnrYNAEKHGLQDA---KKgviFESLPPVLHLQLKRFEY 391

                   .
gi 1907069350  569 N 569
Cdd:COG5077    392 D 392
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
342-566 4.05e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 55.96  E-value: 4.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLF----SLQSFANDLLKQSipwkkipfnalirrfaNLLIKKdICNSE---TKKELLKKVKNAI 414
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlylpKLDELLDDLSKEL----------------KVLKNV-IRKPEpdlNQEEALKLFTALW 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 415 SATAERFSG----YVQNDAHEFLSQCLDQLKEDMEKLNKTWKTePVLGEEnlpdtsatkvftcpvitnlefevQHSIIck 490
Cdd:COG5533    64 SSKEHKVGWippmGSQEDAHELLGKLLDELKLDLVNSFTIRIF-KTTKDK-----------------------KKTST-- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 491 acgetipkrEQFNDLSIDLPRRKKPLPPRSIQDSLDLFfraeeLEYSCEKCGGKCA-----------LVRHKFNRLPRVL 559
Cdd:COG5533   118 ---------GDWFDIIIELPDQTWVNNLKTLQEFIDNM-----EELVDDETGVKAKeneelevqakqEYEVSFVKLPKIL 183

                  ....*..
gi 1907069350 560 ILHLKRY 566
Cdd:COG5533   184 TIQLKRF 190
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
887-931 8.44e-08

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: 55.12  E-value: 8.44e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907069350 887 HSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQ 931
Cdd:cd02668   244 YVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMP 288
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
779-943 1.12e-07

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 54.80  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 779 DENKENKTPEGSQGEVDWLQQYDV-------DREREEQELQQALAQSLQE-------QEAWEQKEDDDLKRATELSLQEF 844
Cdd:cd02666   152 PESMGNQPSVRTKTERFLSLLVDVgkkgreiVVLLEPKDLYDALDRYFDYdsltklpQRSQVQAQLAQPLQRELISMDRY 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 845 NNSFLDSLGSDEDSGNEDVFDMEYTEAEAEELKRNAE-----TGALPHSYRLISVVSHIGSTSSsGHYISDVYDIKKQAW 919
Cdd:cd02666   232 ELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEiekqfDDLKSYGYRLHAVFIHRGEASS-GHYWVYIKDFEENVW 310
                         170       180
                  ....*....|....*....|....
gi 1907069350 920 FTYNDLEVSKIQEAAVQSDRDRSG 943
Cdd:cd02666   311 RKYNDETVTVVPASEVFLFTLGNT 334
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
889-949 1.86e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 53.82  E-value: 1.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069350 889 YRLISVVSHIGSTSSSGHYISDVYDIKKQaWFTYNDLEVSKIQEAAVQSDRdrsGYIFFYM 949
Cdd:cd02661   248 YKLYAVLVHSGFSPHSGHYYCYVKSSNGK-WYNMDDSKVSPVSIETVLSQK---AYILFYI 304
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
887-948 5.32e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 52.50  E-value: 5.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907069350 887 HSYRLISVVSHIGSTSSsGHYISDVYdiKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFY 948
Cdd:COG5533   223 TYYDLVGFVLHQGSLEG-GHYIAYVK--KGGKWEKANDSDVTPVSEEEAINEKAKNAYLYFY 281
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
885-948 3.15e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 50.01  E-value: 3.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069350 885 LPHSYRLISVVSHIGSTSSSGHYisdVYDIKK-----QAWFTYNDLEVSKIQEAAVQSDRdrsGYIFFY 948
Cdd:cd02658   248 GPGKYELIAFISHKGTSVHSGHY---VAHIKKeidgeGKWVLFNDEKVVASQDPPEMKKL---GYIYFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
889-948 4.04e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 50.06  E-value: 4.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 889 YRLISVVSHIGsTSSSGHYISDVYDIKKQaWFTYNDLEVSKIQEAAVQSDRdrsGYIFFY 948
Cdd:cd02660   273 YDLFAVVVHKG-TLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEVLKSQ---AYLLFY 327
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
870-948 5.45e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 49.06  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 870 EAEAEELKRNAE-----TGALPhSYRLISVVSHIGSTSSSGHYISDVYDI-KKQAWFTYNDLEVSKIQEAAVQSDRDRSG 943
Cdd:cd02673   161 IATSDYLKKNEEimkkyCGTDA-KYSLVAVICHLGESPYDGHYIAYTKELyNGSSWLYCSDDEIRPVSKNDVSTNARSSG 239

                  ....*
gi 1907069350 944 YIFFY 948
Cdd:cd02673   240 YLIFY 244
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
889-935 5.61e-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 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: 49.25  E-value: 5.61e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907069350 889 YRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAV 935
Cdd:cd02657   241 YELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDI 287
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-449 1.02e-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 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: 48.48  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 342 GFSNLGNTCYMNAILQSLFS-------LQSFANDLLKQSIPWKKIpFNALIRRFANLLIKKDicnSETKKELLKKVKNAI 414
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSvpelrdaLKNYNPARRGANQSSDNL-TNALRDLFDTMDKKQE---PVPPIEFLQLLRMAF 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907069350 415 SATAER--FSGYVQNDAHEFLSQCLDQLKEDMEKLNK 449
Cdd:cd02657    77 PQFAEKqnQGGYAQQDAEECWSQLLSVLSQKLPGAGS 113
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
889-948 2.52e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 47.30  E-value: 2.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069350 889 YRLISVVSHIGSTSSSGHYISdvydIKKQA--WFTYNDLEVSKIQEAAVQ-----SDRDRSGYIFFY 948
Cdd:cd02663   237 YELVAVVVHIGGGPNHGHYVS----IVKSHggWLLFDDETVEKIDENAVEeffgdSPNQATAYVLFY 299
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
14-99 1.30e-04

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


Pssm-ID: 275390  Cd Length: 89  Bit Score: 41.62  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350  14 SMQTGITKWKEGSFEIVekdnRVSLLVHYNT-GGIPRVFQLSHnIKNVVLRPSGIKQSRLMLTLQD-NSFLSIDKVPSKD 91
Cdd:cd00900     7 RVYREPTKRVEGTLYIT----SDRLILRDKNdGGLELSIPISD-IVNVNVSPQGPSSRYLVLVLKDrGEFVGFSFPKEED 81

                  ....*...
gi 1907069350  92 AEEMRLFL 99
Cdd:cd00900    82 AIEISDAL 89
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
862-952 1.39e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 45.33  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 862 DVFDME-YTEAEA---EELKRNAETGalPHSYRLISVVSHIGsTSSSGHYISDVYDIKKQAWFTYNDLEVSK-----IQE 932
Cdd:cd02659   223 LELDMEpYTEKGLakkEGDSEKKDSE--SYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPfdpndAEE 299
                          90       100
                  ....*....|....*....|
gi 1907069350 933 AAVQSDRDRSGYIFFYMHKE 952
Cdd:cd02659   300 ECFGGEETQKTYDSGPRAFK 319
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
887-949 3.80e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 42.93  E-value: 3.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069350 887 HSYRLISVVSHIGStSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSD-----RDRSGYIFFYM 949
Cdd:cd02665   162 VPYELHAVLVHEGQ-ANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDsfgggRNPSAYCLMYI 228
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
887-932 5.32e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 43.34  E-value: 5.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907069350 887 HSYRLISVVSHIGSTSSSGHYISDVydikkqAWFTYNDLEVSKIQE 932
Cdd:cd02671   270 DVYRLFAVVMHSGATISSGHYTAYV------RWLLFDDSEVKVTEE 309
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
342-385 9.01e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 41.77  E-value: 9.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907069350 342 GFSNLGNTCYMNAILQSLFSLQSFANDLLKQSIPWKKIPFNALI 385
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLFSQQQDVSEFTHLLLDWLEDAFQAAA 44
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
871-948 2.17e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 41.32  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069350 871 AEAEELKRNAETGALPHS---YRLISVVSHIGSTSSSGHYISDVYDIK--------------------KQAWFTYNDLEV 927
Cdd:cd02664   222 PLEKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSESGHYFTYARDQTdadstgqecpepkdaeendeSKNWYLFNDSRV 301
                          90       100
                  ....*....|....*....|....*
gi 1907069350 928 SKIQEAAVQSDRDR----SGYIFFY 948
Cdd:cd02664   302 TFSSFESVQNVTSRfpkdTPYILFY 326
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
885-930 2.30e-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: 41.54  E-value: 2.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907069350 885 LPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKI 930
Cdd:cd02669   379 LSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEV 424
 
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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