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Conserved domains on  [gi|157818981|ref|NP_001100418|]
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ubiquitin carboxyl-terminal hydrolase 26 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH_N pfam16674
N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the ...
3-103 2.74e-45

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: 157.39  E-value: 2.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981    3 PVLIHAQVQLWSAKAGMSKSRNAFIETFIGKREVKLILYFSTGKIKALQLYNNIKSVVLRTYGEDQNYLHLTFKNNDFLF 82
Cdd:pfam16674   1 PLKVHGFVQIWSKKTGMSKWKEAFIEIVEKKKKVKLVVYFNTGGPKTFQLNNNIKSVVLRSYGEKQNRLHLTLKNNSFLF 80
                          90       100
                  ....*....|....*....|.
gi 157818981   83 VEKLTTMDARRLKRFLDKIYQ 103
Cdd:pfam16674  81 IDKLSSTDAEELKMFLDRVHQ 101
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
288-557 6.98e-33

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 129.48  E-value: 6.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  288 GLPNVGNTCYINVVLQSLCSIPLFVnDLFNQGFPWIKPPKDDFNMRL---MQLLVLKDIYNARTRQKLLIGITKALPIFG 364
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSRYNKDINLlcaLRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  365 EVFAADRQNDAHEFLSLCLVQLKETVQRVNMmwqsenesgdyyllreifanytsinRTPVCPVTNNFEFELLSSIFCKAC 444
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHS-------------------------TENESLITDLFRGQLKSRLKCLSC 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  445 GLTVFKREPSRYLSINIP-QGMKDQNMSIQSSLDLFFRAEELEH----RCERClYNKSVAL--HKFGRLPRVIIVHLKRY 517
Cdd:pfam00443 136 GEVSETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDeekyYCDKC-GCKQDAIkqLKISRLPPVLIIHLKRF 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 157818981  518 SFSeSRIMNKDEQHIVISKYLRLSCHCNKNTKPPQPLLPN 557
Cdd:pfam00443 215 SYN-RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
740-805 8.62e-07

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 cd02673:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 245  Bit Score: 50.99  E-value: 8.62e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818981 740 QKEDNIYRLVSIINHIGNSPNGGHYIndAF---DFRKQSWFTYSDLQVTGIQEDLVYKARLSTGYVFFY 805
Cdd:cd02673  178 CGTDAKYSLVAVICHLGESPYDGHYI--AYtkeLYNGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFY 244
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
181-378 6.29e-03

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 COG5077:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 1089  Bit Score: 40.24  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  181 RFFLGAEKEKQNLK-GSTREFETNLVVSISNEKGKERGVraveISKAGFGF-PFETNYpeeGSVNVRDLNDLI--TKLFS 256
Cdd:COG5077    82 SVYLEYEPQELEETgGKYYDCCAQFAFDISNPKYPTIEY----INKSHHRFsMESTDW---GFTNFIDLNKLIepSPGRP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  257 PLLFETHYI----------ENGLDWHEYMEtFLLDPEKSWQGLPNVGNTCYINVVLQSLCSIPLFVNDLFnqGFPWIKP- 325
Cdd:COG5077   155 PFLEEGTLVitvyvrvlkdPTGVLWHSFLN-YNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY--GIPTDHPr 231
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157818981  326 PKDDFNMRLMQLLvlkdiYNARTrQKLLIGITKALPIFGEV-FAADRQNDAHEF 378
Cdd:COG5077   232 GRDSVALALQRLF-----YNLQT-GEEPVDTTELTRSFGWDsDDSFMQHDIQEF 279
 
Name Accession Description Interval E-value
UCH_N pfam16674
N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the ...
3-103 2.74e-45

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: 157.39  E-value: 2.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981    3 PVLIHAQVQLWSAKAGMSKSRNAFIETFIGKREVKLILYFSTGKIKALQLYNNIKSVVLRTYGEDQNYLHLTFKNNDFLF 82
Cdd:pfam16674   1 PLKVHGFVQIWSKKTGMSKWKEAFIEIVEKKKKVKLVVYFNTGGPKTFQLNNNIKSVVLRSYGEKQNRLHLTLKNNSFLF 80
                          90       100
                  ....*....|....*....|.
gi 157818981   83 VEKLTTMDARRLKRFLDKIYQ 103
Cdd:pfam16674  81 IDKLSSTDAEELKMFLDRVHQ 101
PH_USP37_like cd13312
Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37; Members here ...
4-105 1.11e-40

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: 144.76  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981   4 VLIHAQVQLWSAKAGMSKSRNAFIETFIGKREVKLILYFST-GKIKALQLYNNIKSVVLRTYGEDQNYLHLTFKNNDFLF 82
Cdd:cd13312    1 LKIHGFVQIWSKKTGMTKWKEAFIEIVEGKKKVKLVVYFKTgGKPKTFQLSNNIKSVVLRSYGGNQNHLHLTLKNNSFLF 80
                         90       100
                 ....*....|....*....|...
gi 157818981  83 VEKLTTMDARRLKRFLDKIYQSN 105
Cdd:cd13312   81 IDKLSSTDAEQLKEFLDKVHQKK 103
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
288-557 6.98e-33

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 129.48  E-value: 6.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  288 GLPNVGNTCYINVVLQSLCSIPLFVnDLFNQGFPWIKPPKDDFNMRL---MQLLVLKDIYNARTRQKLLIGITKALPIFG 364
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSRYNKDINLlcaLRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  365 EVFAADRQNDAHEFLSLCLVQLKETVQRVNMmwqsenesgdyyllreifanytsinRTPVCPVTNNFEFELLSSIFCKAC 444
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHS-------------------------TENESLITDLFRGQLKSRLKCLSC 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  445 GLTVFKREPSRYLSINIP-QGMKDQNMSIQSSLDLFFRAEELEH----RCERClYNKSVAL--HKFGRLPRVIIVHLKRY 517
Cdd:pfam00443 136 GEVSETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDeekyYCDKC-GCKQDAIkqLKISRLPPVLIIHLKRF 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 157818981  518 SFSeSRIMNKDEQHIVISKYLRLSCHCNKNTKPPQPLLPN 557
Cdd:pfam00443 215 SYN-RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
288-551 1.34e-24

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: 103.72  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSiplfvndlfnqgfpwikppkddfnmrlmqllvlkdiynartrqklligitkalpifgevf 367
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 368 aadRQNDAHEFLSLCLVQLKETVQRVNmmwqsenesgdyyllreifaNYTSINRTPVCPVTNNFEFELLSSIFCKACGLT 447
Cdd:cd02257   21 ---EQQDAHEFLLFLLDKLHEELKKSS--------------------KRTSDSSSLKSLIHDLFGGKLESTIVCLECGHE 77
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 448 VFKREPSRYLSINIPqGMKDQNMSIQSSLDLFFRAEELEHR-CERCLYNKSVALHK---FGRLPRVIIVHLKRYSFSESR 523
Cdd:cd02257   78 SVSTEPELFLSLPLP-VKGLPQVSLEDCLEKFFKEEILEGDnCYKCEKKKKQEATKrlkIKKLPPVLIIHLKRFSFNEDG 156
                        250       260
                 ....*....|....*....|....*...
gi 157818981 524 IMNKDEQHIVISKYLRLSCHCNKNTKPP 551
Cdd:cd02257  157 TKEKLNTKVSFPLELDLSPYLSEGEKDS 184
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
288-466 2.41e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 54.50  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIP----LFVNDLFNQGFPWIKPPKDDFNMRLMQLLVLKDIYNARTRQKLLIGITKALPIF 363
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWelrdYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 364 GEVFAADRQNDAHEFLSLCLVQLKETVQRVNMMWQSENES---GDYYLLR----EIFANYTSINRTpvcPVTNNFEFELL 436
Cdd:COG5560  347 NEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlspGDDVVVKkkakECWWEHLKRNDS---IITDLFQGMYK 423
                        170       180       190
                 ....*....|....*....|....*....|
gi 157818981 437 SSIFCKACGLTVFKREPSRYLSINIPQGMK 466
Cdd:COG5560  424 STLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
740-805 8.62e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 50.99  E-value: 8.62e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818981 740 QKEDNIYRLVSIINHIGNSPNGGHYIndAF---DFRKQSWFTYSDLQVTGIQEDLVYKARLSTGYVFFY 805
Cdd:cd02673  178 CGTDAKYSLVAVICHLGESPYDGHYI--AYtkeLYNGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFY 244
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
181-378 6.29e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 40.24  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  181 RFFLGAEKEKQNLK-GSTREFETNLVVSISNEKGKERGVraveISKAGFGF-PFETNYpeeGSVNVRDLNDLI--TKLFS 256
Cdd:COG5077    82 SVYLEYEPQELEETgGKYYDCCAQFAFDISNPKYPTIEY----INKSHHRFsMESTDW---GFTNFIDLNKLIepSPGRP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  257 PLLFETHYI----------ENGLDWHEYMEtFLLDPEKSWQGLPNVGNTCYINVVLQSLCSIPLFVNDLFnqGFPWIKP- 325
Cdd:COG5077   155 PFLEEGTLVitvyvrvlkdPTGVLWHSFLN-YNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY--GIPTDHPr 231
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157818981  326 PKDDFNMRLMQLLvlkdiYNARTrQKLLIGITKALPIFGEV-FAADRQNDAHEF 378
Cdd:COG5077   232 GRDSVALALQRLF-----YNLQT-GEEPVDTTELTRSFGWDsDDSFMQHDIQEF 279
 
Name Accession Description Interval E-value
UCH_N pfam16674
N-terminal of ubiquitin carboxyl-terminal hydrolase 37; UCH_N is a domain found at the ...
3-103 2.74e-45

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: 157.39  E-value: 2.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981    3 PVLIHAQVQLWSAKAGMSKSRNAFIETFIGKREVKLILYFSTGKIKALQLYNNIKSVVLRTYGEDQNYLHLTFKNNDFLF 82
Cdd:pfam16674   1 PLKVHGFVQIWSKKTGMSKWKEAFIEIVEKKKKVKLVVYFNTGGPKTFQLNNNIKSVVLRSYGEKQNRLHLTLKNNSFLF 80
                          90       100
                  ....*....|....*....|.
gi 157818981   83 VEKLTTMDARRLKRFLDKIYQ 103
Cdd:pfam16674  81 IDKLSSTDAEELKMFLDRVHQ 101
PH_USP37_like cd13312
Pleckstrin homology-like domain of Ubiquitin carboxyl-terminal hydrolase 37; Members here ...
4-105 1.11e-40

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: 144.76  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981   4 VLIHAQVQLWSAKAGMSKSRNAFIETFIGKREVKLILYFST-GKIKALQLYNNIKSVVLRTYGEDQNYLHLTFKNNDFLF 82
Cdd:cd13312    1 LKIHGFVQIWSKKTGMTKWKEAFIEIVEGKKKVKLVVYFKTgGKPKTFQLSNNIKSVVLRSYGGNQNHLHLTLKNNSFLF 80
                         90       100
                 ....*....|....*....|...
gi 157818981  83 VEKLTTMDARRLKRFLDKIYQSN 105
Cdd:cd13312   81 IDKLSSTDAEQLKEFLDKVHQKK 103
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
288-557 6.98e-33

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 129.48  E-value: 6.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  288 GLPNVGNTCYINVVLQSLCSIPLFVnDLFNQGFPWIKPPKDDFNMRL---MQLLVLKDIYNARTRQKLLIGITKALPIFG 364
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFR-DYLLRISPLSEDSRYNKDINLlcaLRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  365 EVFAADRQNDAHEFLSLCLVQLKETVQRVNMmwqsenesgdyyllreifanytsinRTPVCPVTNNFEFELLSSIFCKAC 444
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHS-------------------------TENESLITDLFRGQLKSRLKCLSC 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  445 GLTVFKREPSRYLSINIP-QGMKDQNMSIQSSLDLFFRAEELEH----RCERClYNKSVAL--HKFGRLPRVIIVHLKRY 517
Cdd:pfam00443 136 GEVSETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDeekyYCDKC-GCKQDAIkqLKISRLPPVLIIHLKRF 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 157818981  518 SFSeSRIMNKDEQHIVISKYLRLSCHCNKNTKPPQPLLPN 557
Cdd:pfam00443 215 SYN-RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD 253
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
288-551 1.34e-24

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: 103.72  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSiplfvndlfnqgfpwikppkddfnmrlmqllvlkdiynartrqklligitkalpifgevf 367
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 368 aadRQNDAHEFLSLCLVQLKETVQRVNmmwqsenesgdyyllreifaNYTSINRTPVCPVTNNFEFELLSSIFCKACGLT 447
Cdd:cd02257   21 ---EQQDAHEFLLFLLDKLHEELKKSS--------------------KRTSDSSSLKSLIHDLFGGKLESTIVCLECGHE 77
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 448 VFKREPSRYLSINIPqGMKDQNMSIQSSLDLFFRAEELEHR-CERCLYNKSVALHK---FGRLPRVIIVHLKRYSFSESR 523
Cdd:cd02257   78 SVSTEPELFLSLPLP-VKGLPQVSLEDCLEKFFKEEILEGDnCYKCEKKKKQEATKrlkIKKLPPVLIIHLKRFSFNEDG 156
                        250       260
                 ....*....|....*....|....*...
gi 157818981 524 IMNKDEQHIVISKYLRLSCHCNKNTKPP 551
Cdd:cd02257  157 TKEKLNTKVSFPLELDLSPYLSEGEKDS 184
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-539 1.66e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 86.95  E-value: 1.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNDLFNQGFPWIKPPKDDFNMRLMQLLVLKDIYNARTRQKLLIgITKALPIFGEVF 367
Cdd:cd02661    3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRI-FSSNLKQISKHF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 368 AADRQNDAHEFL--------SLCL---VQLKETVQRvnmmwqseneSGDYYLLREIFANYtsinrtpvcpvtnnfefeLL 436
Cdd:cd02661   82 RIGRQEDAHEFLrylldamqKACLdrfKKLKAVDPS----------SQETTLVQQIFGGY------------------LR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 437 SSIFCKACGLTVFKREPSRYLSINIPQGmkdqnMSIQSSLDLFFRAEELE----HRCERClyNKSVALHK---FGRLPRV 509
Cdd:cd02661  134 SQVKCLNCKHVSNTYDPFLDLSLDIKGA-----DSLEDALEQFTKPEQLDgenkYKCERC--KKKVKASKqltIHRAPNV 206
                        250       260       270
                 ....*....|....*....|....*....|...
gi 157818981 510 IIVHLKRYSFSESRIMNKD---EQHIVISKYLR 539
Cdd:cd02661  207 LTIHLKRFSNFRGGKINKQisfPETLDLSPYMS 239
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-528 3.86e-17

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: 81.57  E-value: 3.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSiplfvndlfnqgfpwikppkddfnmrlmqllvlkdiynartrqklligitkalpifgevf 367
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 368 aadRQNDAHEFLSlclvqlketvqrvnmmwqsenesgdyYLLREIFanytSInrtpvcpVTNNFEFELLSSIFCKACGLT 447
Cdd:cd02674   21 ---DQQDAQEFLL--------------------------FLLDGLH----SI-------IVDLFQGQLKSRLTCLTCGKT 60
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 448 VFKREPSRYLSINIPQGMKDQN-MSIQSSLDLFFRAEELEH----RCERCLYNKSValHK---FGRLPRVIIVHLKRYSF 519
Cdd:cd02674   61 STTFEPFTYLSLPIPSGSGDAPkVTLEDCLRLFTKEETLDGdnawKCPKCKKKRKA--TKkltISRLPKVLIIHLKRFSF 138

                 ....*....
gi 157818981 520 SESRiMNKD 528
Cdd:cd02674  139 SRGS-TRKL 146
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-550 1.17e-16

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 81.59  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSlcsipLFVNDLFNqgfpwikppkddfnmrlmqllVLKDIYNARTRQKLLIGIT------KALP 361
Cdd:cd02663    1 GLENFGNTCYCNSVLQA-----LYFENLLT---------------------CLKDLFESISEQKKRTGVIspkkfiTRLK 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 362 IFGEVFAADRQNDAHEFLSLCLVQLKETVQRVNmmwQSENESGDyyllreifanytsINRTPVCPVTNN-----FEFELL 436
Cdd:cd02663   55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAER---KAEKANRK-------------LNNNNNAEPQPTwvheiFQGILT 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 437 SSIFCKACGLTVFKREPSRYLSINIpqgmkDQNMSIQSSLDLFFRAEELEHR----CERCL----YNKSValhKFGRLPR 508
Cdd:cd02663  119 NETRCLTCETVSSRDETFLDLSIDV-----EQNTSITSCLRQFSATETLCGRnkfyCDECCslqeAEKRM---KIKKLPK 190
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 157818981 509 VIIVHLKRYSFSES-RIMNKDEQHIVISKYLRLSCHCNKNTKP 550
Cdd:cd02663  191 ILALHLKRFKYDEQlNRYIKLFYRVVFPLELRLFNTTDDAENP 233
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-521 3.49e-14

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: 74.28  E-value: 3.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNDLFNQGFPWIKPPKD---DFNMRLMQLL-------VLKDIYNARTRQKLLIGIT 357
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpanDLNCQLIKLAdgllsgrYSKPASLKSENDPYQVGIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 358 ----KALpIFG--EVFAADRQNDAHEFLSlclvQLKETVQRvnmmwqsenesgdyyllreifanytSINRTPVCPVTNNF 431
Cdd:cd02658   81 psmfKAL-IGKghPEFSTMRQQDALEFLL----HLIDKLDR-------------------------ESFKNLGLNPNDLF 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 432 EFELLSSIFCKACGLTVFKREPSRYLSINIP---------QGMKDQNMSIQSSLDLFFRAEELEHRCERClYNKSVALH- 501
Cdd:cd02658  131 KFMIEDRLECLSCKKVKYTSELSEILSLPVPkdeatekeeGELVYEPVPLEDCLKAYFAPETIEDFCSTC-KEKTTATKt 209
                        250       260
                 ....*....|....*....|.
gi 157818981 502 -KFGRLPRVIIVHLKRYSFSE 521
Cdd:cd02658  210 tGFKTFPDYLVINMKRFQLLE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
287-544 3.81e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 71.25  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 287 QGLPNVGNTCYINVVLQSLCSIPLFVNDLFNQG---FPWIKPPKDDFNMRlMQLLVLKDIYNARTRQKLLIGITKALPIF 363
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRhscTCLSCSPNSCLSCA-MDEIFQEFYYSGDRSPYGPINLLYLSWKH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 364 GEVFAADRQNDAHEFlslclvqlketvqrvnmmWQsenesgdyYLLREIFANYTSINRTPV------CPVTNNFEFELLS 437
Cdd:cd02660   80 SRNLAGYSQQDAHEF------------------FQ--------FLLDQLHTHYGGDKNEANdeshcnCIIHQTFSGSLQS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 438 SIFCKACGLTVFKREPSRYLSINIP-QGMK---------DQNMSIQSSLDLFFRAEELE---HRCERClYNKSVALHKFG 504
Cdd:cd02660  134 SVTCQRCGGVSTTVDPFLDLSLDIPnKSTPswalgesgvSGTPTLSDCLDRFTRPEKLGdfaYKCSGC-GSTQEATKQLS 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 157818981 505 --RLPRVIIVHLKRYSFSESRIMNKDEQHIVISKYLRLSCHC 544
Cdd:cd02660  213 ikKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPYT 254
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-538 1.73e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 67.78  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNdlfnqgfpWIKppkddfnmRLMQllvlkdiynartrqklligitkalpifgevf 367
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIE--------YLE--------EFLE------------------------------- 33
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 368 aadrQNDAHEFLSLCLVQLketvqrvnmmwqsENEsgdyyllreifanytsinrtpvcpVTNNFEFELLSSIFCKACGLT 447
Cdd:cd02662   34 ----QQDAHELFQVLLETL-------------EQL------------------------LKFPFDGLLASRIVCLQCGES 72
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 448 VFKREPSRY-LSINIPQGMKDQNMSIQSSLDLFFRAEELE-HRCERCLynksvalHKFGRLPRVIIVHLKRYSFSESRIM 525
Cdd:cd02662   73 SKVRYESFTmLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDdYKCDRCQ-------TVIVRLPQILCIHLSRSVFDGRGTS 145
                        250
                 ....*....|....*..
gi 157818981 526 NKDEQHI----VISKYL 538
Cdd:cd02662  146 TKNSCKVsfpeRLPKVL 162
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-519 2.65e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 65.74  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNDLFNQgfPWIKPPKDDFN-MRLMQLLVL------KDIYNARTRQKlligiTKAL 360
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSI--PPTEDDDDNKSvPLALQRLFLflqlseSPVKTTELTDK-----TRSF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 361 PifGEVFAADRQNDAHEFLSLCLVQLKEtvqrvnMMWQSENESgdyyllreifanytSINRTpvcpvtnnFEFELLSSIF 440
Cdd:cd02659   77 G--WDSLNTFEQHDVQEFFRVLFDKLEE------KLKGTGQEG--------------LIKNL--------FGGKLVNYII 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 441 CKACGLTVFKREPSRYLSINIpQGMKdqnmSIQSSLDLFFRAEELE----HRCERClyNKSVALHK---FGRLPRVIIVH 513
Cdd:cd02659  127 CKECPHESEREEYFLDLQVAV-KGKK----NLEESLDAYVQGETLEgdnkYFCEKC--GKKVDAEKgvcFKKLPPVLTLQ 199

                 ....*.
gi 157818981 514 LKRYSF 519
Cdd:cd02659  200 LKRFEF 205
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-540 1.50e-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: 63.28  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNDLFNQGFPWIKP---PKDDFNMRLMQLLVLKDIYNARTRQKLLigitKALPifg 364
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDsqsVMKKLQLLQAHLMHTQRRAEAPPDYFLE----ASRP--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 365 EVFAADRQNDAHEFLSLCLVQLKETVQRVnmmwqsenesgdyyllreifanytsinrtpvcpvtnnFEFELLSSIFCKAC 444
Cdd:cd02664   74 PWFTPGSQQDCSEYLRYLLDRLHTLIEKM-------------------------------------FGGKLSTTIRCLNC 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 445 GLTVFKREPSRYLSINIPqgmkdqnmSIQSSLDLFFRAEEL----EHRCERCLYNKSVALH-KFGRLPRVIIVHLKRYSF 519
Cdd:cd02664  117 NSTSARTERFRDLDLSFP--------SVQDLLNYFLSPEKLtgdnQYYCEKCASLQDAEKEmKVTGAPEYLILTLLRFSY 188
                        250       260
                 ....*....|....*....|....*.
gi 157818981 520 SESR-----IMNKdeqhIVISKYLRL 540
Cdd:cd02664  189 DQKThvrekIMDN----VSINEVLSL 210
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-532 8.69e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 60.48  E-value: 8.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPlFVNDLFNqgfpwikppkddfnmrlmqllvlkdiynaRTRQKLLIGITKALPIFGEVf 367
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTP-ALRELLS-----------------------------ETPKELFSQVCRKAPQFKGY- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 368 aadRQNDAHEFLSLCLVQLKETVQRVnmmwqsenesgdyyllreifanytsinrtpvcpvtnnFEFELLSSIFCKACGLT 447
Cdd:cd02667   50 ---QQQDSHELLRYLLDGLRTFIDSI-------------------------------------FGGELTSTIMCESCGTV 89
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 448 VFKREPSRYLSINIPQGMKDQNmSIQSSLDLFFRAEELE----HRCERCLYNKSVALhkFGRLPRVIIVHLKRYSFSESR 523
Cdd:cd02667   90 SLVYEPFLDLSLPRSDEIKSEC-SIESCLKQFTEVEILEgnnkFACENCTKAKKQYL--ISKLPPVLVIHLKRFQQPRSA 166

                 ....*....
gi 157818981 524 IMNKDEQHI 532
Cdd:cd02667  167 NLRKVSRHV 175
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
285-550 9.03e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 57.98  E-value: 9.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 285 SWQGLPNVGNTCYINVVLQSLCSIPLF---VNDLFNQGfpwikppkddFNMRLMQL--LVLKDIYNARTRQKLLIGITKA 359
Cdd:cd02671   23 PFVGLNNLGNTCYLNSVLQVLYFCPGFkhgLKHLVSLI----------SSVEQLQSsfLLNPEKYNDELANQAPRRLLNA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 360 LPIFGEVFAADRQNDAHEFLSLCLVQLKETVQRvnmMWQSENESGDYYLLREIFANYTSINRTPVCPVTnnfEFELLSSi 439
Cdd:cd02671   93 LREVNPMYEGYLQHDAQEVLQCILGNIQELVEK---DFQGQLVLRTRCLECETFTERREDFQDISVPVQ---ESELSKS- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 440 fckacgltvfkrEPSRYLSINIPQGMKDQNMSIQSsldlFFRAE----ELEHRCERCL-YNKSVALHKFGRLPRVIIVHL 514
Cdd:cd02671  166 ------------EESSEISPDPKTEMKTLKWAISQ----FASVErivgEDKYFCENCHhYTEAERSLLFDKLPEVITIHL 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 157818981 515 KRYSFSESRI-----MNKDEQHIVISkyLRLSCH--CNKNTKP 550
Cdd:cd02671  230 KCFAANGSEFdcyggLSKVNTPLLTP--LKLSLEewSTKPKND 270
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
288-466 2.41e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 54.50  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIP----LFVNDLFNQGFPWIKPPKDDFNMRLMQLLVLKDIYNARTRQKLLIGITKALPIF 363
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWelrdYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 364 GEVFAADRQNDAHEFLSLCLVQLKETVQRVNMMWQSENES---GDYYLLR----EIFANYTSINRTpvcPVTNNFEFELL 436
Cdd:COG5560  347 NEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlspGDDVVVKkkakECWWEHLKRNDS---IITDLFQGMYK 423
                        170       180       190
                 ....*....|....*....|....*....|
gi 157818981 437 SSIFCKACGLTVFKREPSRYLSINIPQGMK 466
Cdd:COG5560  424 STLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
740-805 8.62e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 50.99  E-value: 8.62e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818981 740 QKEDNIYRLVSIINHIGNSPNGGHYIndAF---DFRKQSWFTYSDLQVTGIQEDLVYKARLSTGYVFFY 805
Cdd:cd02673  178 CGTDAKYSLVAVICHLGESPYDGHYI--AYtkeLYNGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFY 244
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
289-542 2.25e-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: 49.83  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 289 LPNVGNTCYINVVLQSLCSIPLFVNDlfnqgfpwikppkddfnmrlmqllvlkdiynartrqklligitkalpifgevFA 368
Cdd:cd02673    2 LVNTGNSCYFNSTMQALSSIGKINTE----------------------------------------------------FD 29
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 369 ADRQNDAHEFLSlclvqlkETVQRVNMMWQSENEsgdyyllREIFANYTSINRTPVcpvtNNFEFELLSSIFCKACGltv 448
Cdd:cd02673   30 NDDQQDAHEFLL-------TLLEAIDDIMQVNRT-------NVPPSNIEIKRLNPL----EAFKYTIESSYVCIGCS--- 88
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 449 fKREPSRYLSINIPQGMKDQNMSIQSSLDL-FFRAEELEHRCERCLYNKSVALHKFGRLPRVIIVHLKRYSFSESrimnk 527
Cdd:cd02673   89 -FEENVSDVGNFLDVSMIDNKLDIDELLISnFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRYKLRIA----- 162
                        250
                 ....*....|....*
gi 157818981 528 deqhivISKYLRLSC 542
Cdd:cd02673  163 ------TSDYLKKNE 171
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
288-387 1.28e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 47.87  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLcsiplfvndLFNQgfPWIKPPKDDfnmRLMQLLVLKDIYNARTRQKLLIGITKAL------- 360
Cdd:COG5533    1 GLPNLGNTCFMNSVLQIL---------ALYL--PKLDELLDD---LSKELKVLKNVIRKPEPDLNQEEALKLFtalwssk 66
                         90       100
                 ....*....|....*....|....*...
gi 157818981 361 -PIFGEVFAADRQNDAHEFLSLCLVQLK 387
Cdd:COG5533   67 eHKVGWIPPMGSQEDAHELLGKLLDELK 94
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-788 5.72e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 45.87  E-value: 5.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818981 735 PQKLNQKE--------DNIYRLVSIINHIGNSPNGGHYINDAFDFRKQSWFTYSDLQVTGIQ 788
Cdd:cd02668  227 PEILDMGEylaesdegSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMP 288
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-518 9.64e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 45.77  E-value: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNDLFNQGFP-WIKPPKDDFNMRLMQLlvLKDIYNAR------TRQKLLIGITKAL 360
Cdd:cd02669  121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYeNIKDRKSELVKRLSEL--IRKIWNPRnfkghvSPHELLQAVSKVS 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 361 pifGEVFAADRQNDAHEFLSLCLVQLKETVQRVNmmwqSENESgdyyLLREIFANYTSINRTPVCPVTNNfefELLSSIF 440
Cdd:cd02669  199 ---KKKFSITEQSDPVEFLSWLLNTLHKDLGGSK----KPNSS----IIHDCFQGKVQIETQKIKPHAEE---EGSKDKF 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 441 CKACGLTVFKREPSRYLSINIP-----QGMKDQNMSIQSSL-DLF--FRAEELEHrcerclYNKSVALHKFGRLPRVIIV 512
Cdd:cd02669  265 FKDSRVKKTSVSPFLLLTLDLPppplfKDGNEENIIPQVPLkQLLkkYDGKTETE------LKDSLKRYLISRLPKYLIF 338

                 ....*.
gi 157818981 513 HLKRYS 518
Cdd:cd02669  339 HIKRFS 344
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
746-805 1.41e-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: 44.62  E-value: 1.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157818981 746 YRLVSIINHIGNSPNGGHYIndAF----DFRKQSWFTYSDLQVTGIQEDLVYKarlSTGYVFFY 805
Cdd:cd02658  252 YELIAFISHKGTSVHSGHYV--AHikkeIDGEGKWVLFNDEKVVASQDPPEMK---KLGYIYFY 310
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-519 2.81e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 43.95  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSlcsipLFVNDLFNQGF--------------PWIKPPKDDFNMRLMQLLVLKDIYNartRQKLL 353
Cdd:cd02668    1 GLKNLGATCYVNSFLQL-----WFMNLEFRKAVyecnstedaelknmPPDKPHEPQTIIDQLQLIFAQLQFG---NRSVV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 354 --IGITKALPIFGEVfaadrQNDAHEFLSLCLVQLKETVQrvnmmwQSENESGDYYLLREIFANYTSINRtpvcpvtnnf 431
Cdd:cd02668   73 dpSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLS------KSKNPDLKNIVQDLFRGEYSYVTQ---------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 432 efellssifCKACGLTvfKREPSRY--LSINIpQGMKdqnmSIQSSLDLFFRAEELE----HRCERCLYN----KSVALH 501
Cdd:cd02668  132 ---------CSKCGRE--SSLPSKFyeLELQL-KGHK----TLEECIDEFLKEEQLTgdnqYFCESCNSKtdatRRIRLT 195
                        250
                 ....*....|....*...
gi 157818981 502 kfgRLPRVIIVHLKRYSF 519
Cdd:cd02668  196 ---TLPPTLNFQLLRFVF 210
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
288-522 1.22e-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 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: 41.93  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 288 GLPNVGNTCYINVVLQSLCSIPLFVNDLFNQGfpwikpPKDDFNMRLMQLLV--LKDIYNA--RTRQ-----KLLIGITK 358
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYN------PARRGANQSSDNLTnaLRDLFDTmdKKQEpvppiEFLQLLRM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 359 ALPIFGEV--FAADRQNDAHEflslCLVQLKETVQRVNMMWQSENESGDYYllreifanytsinrtpvcpvtnnFEFELL 436
Cdd:cd02657   75 AFPQFAEKqnQGGYAQQDAEE----CWSQLLSVLSQKLPGAGSKGSFIDQL-----------------------FGIELE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981 437 SSIFCKACGL-TVFKREPSRYLSINIpqGMKDQNMSIQSSLDLFFRaEELEHRCERC----LYNKSvalHKFGRLPRVII 511
Cdd:cd02657  128 TKMKCTESPDeEEVSTESEYKLQCHI--SITTEVNYLQDGLKKGLE-EEIEKHSPTLgrdaIYTKT---SRISRLPKYLT 201
                        250
                 ....*....|.
gi 157818981 512 VHLKRYSFSES 522
Cdd:cd02657  202 VQFVRFFWKRD 212
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
181-378 6.29e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 40.24  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  181 RFFLGAEKEKQNLK-GSTREFETNLVVSISNEKGKERGVraveISKAGFGF-PFETNYpeeGSVNVRDLNDLI--TKLFS 256
Cdd:COG5077    82 SVYLEYEPQELEETgGKYYDCCAQFAFDISNPKYPTIEY----INKSHHRFsMESTDW---GFTNFIDLNKLIepSPGRP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818981  257 PLLFETHYI----------ENGLDWHEYMEtFLLDPEKSWQGLPNVGNTCYINVVLQSLCSIPLFVNDLFnqGFPWIKP- 325
Cdd:COG5077   155 PFLEEGTLVitvyvrvlkdPTGVLWHSFLN-YNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVY--GIPTDHPr 231
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157818981  326 PKDDFNMRLMQLLvlkdiYNARTrQKLLIGITKALPIFGEV-FAADRQNDAHEF 378
Cdd:COG5077   232 GRDSVALALQRLF-----YNLQT-GEEPVDTTELTRSFGWDsDDSFMQHDIQEF 279
 
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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