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Conserved domains on  [gi|114053325|ref|NP_570949|]
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ubiquitin carboxyl-terminal hydrolase 48 isoform 1 [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119314)

ubiquitin carboxyl-terminal hydrolase family protein may remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-418 0e+00

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


:

Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 568.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668    79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668   159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668   239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314

                         330
                  ....*....|
gi 114053325  409 SRNAYMLVYR 418
Cdd:cd02668   315 SRTAYMLVYK 324
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 956-1051 3.19e-40

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


:

Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 143.58  E-value: 3.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  956 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1032
Cdd:cd01795     1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80

                          90
                  ....*....|....*....
gi 114053325 1033 DVMQVCMPEEGFKGTGLLG 1051
Cdd:cd01795    81 DVSRARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 483-553 9.04e-10

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


:

Pssm-ID: 399383  Cd Length: 80  Bit Score: 56.22  E-value: 9.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114053325   483 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAANIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337    2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-418 0e+00

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 568.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668    79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668   159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668   239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314

                         330
                  ....*....|
gi 114053325  409 SRNAYMLVYR 418
Cdd:cd02668   315 SRTAYMLVYK 324
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-417 1.01e-60

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 209.99  E-value: 1.01e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325    89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIHggkdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYE 238
Cdd:pfam00443   72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   239 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443  148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   313 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKmegkklqlgIE 387
Cdd:pfam00443  226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTE---------VD 295

                          330       340       350
                   ....*....|....*....|....*....|
gi 114053325   388 EDLEPSksqtrkpkcgkgthcSRNAYMLVY 417
Cdd:pfam00443  296 EETAVL---------------SSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 72-457 1.11e-45

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 179.30  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   72 FHSIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgihgGKDyepqTICEHLQYL 151
Cdd:COG5077   179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077   244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077   320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  309 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMegkklq 383
Cdd:COG5077   399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRA------ 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  384 lGIEEDLEPSKSQTR--KPKCGKGTHCSR--NAYMLVYRLQAQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 454
Cdd:COG5077   472 -TEKEVLEENFGGDHpyKDKIRDHSGIKRfmSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549


                  ...
gi 114053325  455 EMR 457
Cdd:COG5077   550 EIH 552
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 956-1051 3.19e-40

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 143.58  E-value: 3.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  956 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1032
Cdd:cd01795     1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80

                          90
                  ....*....|....*....
gi 114053325 1033 DVMQVCMPEEGFKGTGLLG 1051
Cdd:cd01795    81 DVSRARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 483-553 9.04e-10

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 56.22  E-value: 9.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114053325   483 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAANIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337    2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
DUSP smart00695
Domain in ubiquitin-specific proteases;
482-555 9.83e-06

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 45.04  E-value: 9.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325    482 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAANIFYSRYGGGPR-LTVKA 551
Cdd:smart00695    5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84


                    ....
gi 114053325    552 LCKD 555
Cdd:smart00695   85 VCQG 88
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 961-1019 1.14e-05

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 44.17  E-value: 1.14e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 114053325    961 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1019
Cdd:smart00213   12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 966-1019 1.23e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 38.31  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 114053325   966 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1019
Cdd:pfam00240   15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-418 0e+00

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 568.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYtkGDGIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFV 169
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAE--LKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 KALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQL 249
Cdd:cd02668    79 KALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  250 TDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPY-VE 328
Cdd:cd02668   159 EECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYlAE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  329 HKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKLQLGIEEDlepsKSQTRKPKCGKGTHC 408
Cdd:cd02668   239 SDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSED----PAKPRKSEIKKGTHS 314

                         330
                  ....*....|
gi 114053325  409 SRNAYMLVYR 418
Cdd:cd02668   315 SRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 88-418 1.77e-79

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: 262.96  E-value: 1.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   88 FVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgihGGKDYEPQTICeHLQYLFALLQNSNRRYIDPSG 167
Cdd:cd02659     2 YVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-----------EDDDDNKSVPL-ALQRLFLFLQLSESPVKTTEL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLskqKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELN 242
Cdd:cd02659    70 TDKTRSfgwdsLNTFEQHDVQEFFRVLFDKLEEKL---KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  243 IQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLD 322
Cdd:cd02659   147 VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  323 MEPYVEH------------KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKM---EGKKLQLGIE 387
Cdd:cd02659   227 MEPYTEKglakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnDAEEECFGGE 305

                         330       340       350
                  ....*....|....*....|....*....|.
gi 114053325  388 EDLEPSKSQTRKpkcGKGTHcsrNAYMLVYR 418
Cdd:cd02659   306 ETQKTYDSGPRA---FKRTT---NAYMLFYE 330
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
89-417 1.01e-60

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 209.99  E-value: 1.01e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325    89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIHggkdyepqtICEHLQYLF-ALLQNSNRRYIDPSG 167
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------LLCALRDLFkALQKNSKSSSVSPKM 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   168 FVKALG-----LDTGQQQDAQEFsklFMSLLeDTLSKQKNPD----VRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYE 238
Cdd:pfam00443   72 FKKSLGklnpdFSGYKQQDAQEF---LLFLL-DGLHEDLNGNhsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   239 LELNIQGHK------QLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLN 312
Cdd:pfam00443  148 LSLPIPGDSaelktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLN 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   313 AYIGFSESLDMEPYV-----EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKmegkklqlgIE 387
Cdd:pfam00443  226 TEVEFPLELDLSRYLaeelkPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTE---------VD 295

                          330       340       350
                   ....*....|....*....|....*....|
gi 114053325   388 EDLEPSksqtrkpkcgkgthcSRNAYMLVY 417
Cdd:pfam00443  296 EETAVL---------------SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 90-418 6.13e-58

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: 200.02  E-value: 6.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNtflqvwflnlelrqalylcpSTcsdytkgdgihggkdyepqticehLQYLFAllqnsnrryidpsgfv 169
Cdd:cd02257     1 GLNNLGNTCYLN--------------------SV------------------------LQALFS---------------- 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 kalgldtgQQQDAQEFSKLFMSLLEDTLSKQKNPDV-----RNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQ 244
Cdd:cd02257    21 --------EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  245 GHKQ----LTDCISEFLKEERLEGDNRYFCEnCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSES 320
Cdd:cd02257    93 VKGLpqvsLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  321 LDMEPYVEHKG-------GSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgiEEDLEps 393
Cdd:cd02257   171 LDLSPYLSEGEkdsdsdnGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVS--------EEEVL-- 240

                         330       340
                  ....*....|....*....|....*
gi 114053325  394 ksqtrkpkcgKGTHCSRNAYMLVYR 418
Cdd:cd02257   241 ----------EFGSLSSSAYILFYE 255
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 72-457 1.11e-45

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 179.30  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   72 FHSIDDPNceRRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDytkgdgihgGKDyepqTICEHLQYL 151
Cdd:COG5077   179 WHSFLNYN--SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPR---------GRD----SVALALQRL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  152 FALLQNSNRRyIDPSGFVKALGLDTGQ---QQDAQEFSKLFMSLLEDTLSKQKnpdVRNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:COG5077   244 FYNLQTGEEP-VDTTELTRSFGWDSDDsfmQHDIQEFNRVLQDNLEKSMRGTV---VENALNGIFVGKMKSYIKCVNVNY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENcQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:COG5077   320 ESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMM 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  309 KKLNAYIGFSESLDMEPYVEH-----KGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMegkklq 383
Cdd:COG5077   399 VKINDRYEFPLEIDLLPFLDRdadksENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEKDGRWYKFDDTRVTRA------ 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  384 lGIEEDLEPSKSQTR--KPKCGKGTHCSR--NAYMLVYRLQAQEkNHTM-----VQVPAFLQELVDRDNSKFEEWCVEMA 454
Cdd:COG5077   472 -TEKEVLEENFGGDHpyKDKIRDHSGIKRfmSAYMLVYLRKSML-DDLLnpvaaVDIPPHVEEVLSEEIDKTEVRCKEID 549


                  ...
gi 114053325  455 EMR 457
Cdd:COG5077   550 EIH 552
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 178-418 4.30e-43

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: 156.68  E-value: 4.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  178 QQQDAQEFsklfMSLLEDTLskqknpdvRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNI-----QGHKQ-LTD 251
Cdd:cd02674    21 DQQDAQEF----LLFLLDGL--------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgDAPKVtLED 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  252 CISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFS-ESLDMEPYV--E 328
Cdd:cd02674    89 CLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPlNDLDLTPYVdtR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  329 HKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEgkklqlgieedlepsksqtrkpkcgKGTHC 408
Cdd:cd02674   167 SFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNETNDWYKFDDSRVTKVS-------------------------ESSVV 220

                         250
                  ....*....|
gi 114053325  409 SRNAYMLVYR 418
Cdd:cd02674   221 SSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-417 6.95e-43

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: 158.59  E-value: 6.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVwflnleLRQALYL---CPStcSDYTKGDGIHGGKdyepqTICEHLQYLFALLQNSnRRYIDPS 166
Cdd:cd02661     3 GLQNLGNTCFLNSVLQC------LTHTPPLanyLLS--REHSKDCCNEGFC-----MMCALEAHVERALASS-GPGSAPR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  167 GFVKAL-----GLDTGQQQDAQEFSKLFMSLLE----DTLSKQKNPDVR----NVVQQQFCGEYAYVTVCNQCGRESKLV 233
Cdd:cd02661    69 IFSSNLkqiskHFRIGRQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSsqetTLVQQIFGGYLRSQVKCLNCKHVSNTY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  234 SKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRqtGHkkKLNA 313
Cdd:cd02661   149 DPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  314 YIGFSESLDMEPYV-EHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPqSGEWYKFNDEDIEKMEgkklqlgiEEDLep 392
Cdd:cd02661   225 QISFPETLDLSPYMsQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS-NGKWYNMDDSKVSPVS--------IETV-- 293

                         330       340
                  ....*....|....*....|....*
gi 114053325  393 sksqtrkpkcgkgthCSRNAYMLVY 417
Cdd:cd02661   294 ---------------LSQKAYILFY 303
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 956-1051 3.19e-40

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 143.58  E-value: 3.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  956 RKVRGE-KALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMD-- 1032
Cdd:cd01795     1 RRVRGErKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADea 80

                          90
                  ....*....|....*....
gi 114053325 1033 DVMQVCMPEEGFKGTGLLG 1051
Cdd:cd01795    81 DVSRARVPEEGFKGTALLG 99
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 3.70e-39

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 148.79  E-value: 3.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgIHGGKDYEPQTICEHLQYLFALLQNSNRRYIDP-SGF 168
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-------------LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpDYF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  169 VKAL---GLDTGQQQDAQEFSKLFMSLLeDTLskqknpdvrnvVQQQFCGEYAYVTVCNQCGRESKLVSKFYELELNIqg 245
Cdd:cd02664    68 LEASrppWFTPGSQQDCSEYLRYLLDRL-HTL-----------IEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  246 hKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEP 325
Cdd:cd02664   134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPV 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  326 YVEHKGGSFV--------------------YELSAVLIHRGVSAYSGHYIAHVKDPQSGE-------------------- 365
Cdd:cd02664   213 RVESKSSESPlekkeeesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDADstgqecpepkdaeendeskn 292


                  ....*.
gi 114053325  366 WYKFND 371
Cdd:cd02664   293 WYLFND 298
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-379 8.77e-36

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 138.23  E-value: 8.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALylcpstcSDYTkgdGIHGGKDYEPQTICEHLQYLFALLQNSNRRyIDPSGFV 169
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-------KNYN---PARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 KALGL---------DTGQ--QQDAQE-FSKLFMSLledTLSKQKNPDVRNVVQQQFCGEYAYVTVC-NQCGRESKLVSKF 236
Cdd:cd02657    70 QLLRMafpqfaekqNQGGyaQQDAEEcWSQLLSVL---SQKLPGAGSKGSFIDQLFGIELETKMKCtESPDEEEVSTESE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  237 YELELNIqGHKQLTDCISEFLKEeRLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIG 316
Cdd:cd02657   147 YKLQCHI-SITTEVNYLQDGLKK-GLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114053325  317 FSESLDMEPYVEHKGgsfVYELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYKFND--------EDIEKMEG 379
Cdd:cd02657   225 FPFELDLYELCTPSG---YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDdkvsevteEDILKLSG 292
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-371 3.61e-35

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: 137.12  E-value: 3.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVwFLNLELRQALYLcpstcSDytkGDGIHGGKDYEPQTICEHLQYLFA-LLQNSNRRyidPSGF 168
Cdd:cd02660     2 GLINLGATCFMNVILQA-LLHNPLLRNYFL-----SD---RHSCTCLSCSPNSCLSCAMDEIFQeFYYSGDRS---PYGP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  169 VKAL--------GLDTGQQQDAQEFsklFMSLLE--------DTLSKQKNPDVRNVVQQQFCGEYAYVTVCNQCGRESKL 232
Cdd:cd02660    70 INLLylswkhsrNLAGYSQQDAHEF---FQFLLDqlhthyggDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  233 VSKFYELELNIQGHKQ---------------LTDCISEFLKEERLeGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLM 297
Cdd:cd02660   147 VDPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  298 RFVFDrQTGHKKKLNAYIGFSESLDMEPYV----------EHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKDpQSGEWY 367
Cdd:cd02660   226 RFEHS-LNKTSRKIDTYVQFPLELNMTPYTsssigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQ-GDGQWF 302


                  ....
gi 114053325  368 KFND 371
Cdd:cd02660   303 KFDD 306
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-417 3.70e-35

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: 136.29  E-value: 3.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNlelrqALYLCpstcsdytkgdgihggkdyepqticehLQYLFALLQNSNRRY--IDPSG 167
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFE-----NLLTC---------------------------LKDLFESISEQKKRTgvISPKK 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  168 FVKALG-----LDTGQQQDAQEFSKLFMSLLEDTLSKQK--------------NPDVRNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:cd02663    49 FITRLKrenelFDNYMHQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnAEPQPTWVHEIFQGILTNETRCLTCET 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  229 ESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHK 308
Cdd:cd02663   129 VSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRY 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  309 KKLNAYIGFSESL------DMEPYVEHKggsfvYELSAVLIHRGVSAYSGHYIAHVKdpQSGEWYKFNDEDIEKMEGKKl 382
Cdd:cd02663   209 IKLFYRVVFPLELrlfnttDDAENPDRL-----YELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENA- 280

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 114053325  383 qlgIEEDLEPSKSQTrkpkcgkgthcsrNAYMLVY 417
Cdd:cd02663   281 ---VEEFFGDSPNQA-------------TAYVLFY 299
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 78-400 2.99e-31

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: 125.78  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   78 PNCERRKKN--SFVGLTNLGATCYVNTFLQVwflnlelrqaLYLCPSTCSDYTKGDGIHGGKdyepqticEHLQYLFALL 155
Cdd:cd02671    12 ATSCEKRENllPFVGLNNLGNTCYLNSVLQV----------LYFCPGFKHGLKHLVSLISSV--------EQLQSSFLLN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  156 Q---NSNRRYIDPSGFVKALG-----LDTGQQQDAQEFsklFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCNQCG 227
Cdd:cd02671    74 PekyNDELANQAPRRLLNALRevnpmYEGYLQHDAQEV---LQCILGN---------IQELVEKDFQGQLVLRTRCLECE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  228 ----------------RESKLVSKFYELELNIQGH---KQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSL 288
Cdd:cd02671   142 tfterredfqdisvpvQESELSKSEESSEISPDPKtemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  289 PCTLNLQLMRF----VFDRQTGHKKKLNAYIGFSESLDMEPYVEhKGGSFVYELSAVLIHRGVSAYSGHYIAHVKdpqsg 364
Cdd:cd02671   222 PEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWST-KPKNDVYRLFAVVMHSGATISSGHYTAYVR----- 295

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 114053325  365 eWYKFNDEDIEKMEgkklQLGIEEDLEPSKSQTRKP 400
Cdd:cd02671   296 -WLLFDDSEVKVTE----EKDFLEALSPNTSSTSTP 326
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-372 9.15e-30

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 120.89  E-value: 9.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFlNLELRQALYLC-----------PSTC--SDYTK-GDGIHGGKDYEPQTICEHlqylfall 155
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLF-SIPSFQWRYDDlenkfpsdvvdPANDlnCQLIKlADGLLSGRYSKPASLKSE-------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  156 QNSNRRYIDPSGFVKALG-----LDTGQQQDAQEFSKLFMSLLED----TLSKQKNPDVRNVVQQQFCgeyayvtvCNQC 226
Cdd:cd02658    72 NDPYQVGIKPSMFKALIGkghpeFSTMRQQDALEFLLHLIDKLDResfkNLGLNPNDLFKFMIEDRLE--------CLSC 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  227 GRESKLVSKFYELELNIQGHKQ--------------LTDCISEFLKEERLEgdnrYFCENCQSKQNATRKIRLLSLPCTL 292
Cdd:cd02658   144 KKVKYTSELSEILSLPVPKDEAtekeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  293 NLQLMRFVFDrQTGHKKKLNAYIGFSESLDMEPYvehkggsfvyELSAVLIHRGVSAYSGHYIAHVK--DPQSGEWYKFN 370
Cdd:cd02658   220 VINMKRFQLL-ENWVPKKLDVPIDVPEELGPGKY----------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFN 288


                  ..
gi 114053325  371 DE 372
Cdd:cd02658   289 DE 290
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-374 2.02e-28

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 115.95  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTcsdytkgdgihggkdyepqticehlqyLFALLQNSNRRYIDpsgfv 169
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE---------------------------LFSQVCRKAPQFKG----- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 kalgldtGQQQDAQEfskLFMSLLEDtlskqknpdVRNVVQQQFCGEYAYVTVCNQCGRESKLVSKFYELEL----NIQG 245
Cdd:cd02667    49 -------YQQQDSHE---LLRYLLDG---------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  246 HKQLTDCISEFLKEERLEGDNRYFCENCQskqNATRKIRLLSLPCTLNLQLMRFVFDRQTGhKKKLNAYIGFSESLDMEP 325
Cdd:cd02667   110 ECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAN-LRKVSRHVSFPEILDLAP 185

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114053325  326 Y------VEHKGGSFVYELSAVLIHRGvSAYSGHYIAHVKD---------------------PQSGEWYKFNDEDI 374
Cdd:cd02667   186 FcdpkcnSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDV 260
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
89-371 1.84e-19

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 90.41  E-value: 1.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325    89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCpsTCSDYTKgdgihggkdyEPQTICEhLQYLFALLQNSNRRYIDPSGF 168
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSH--LATECLK----------EHCLLCE-LGFLFDMLEKAKGKNCQASNF 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   169 VKALG----------LDTGQQQDA--------QEFSKLFMS-LLEDTLSKQKNPDV-RNVVQQQFCGEYAYVTVCNQCGR 228
Cdd:pfam13423   68 LRALSsipeasalglLDEDRETNSaislssliQSFNRFLLDqLSSEENSTPPNPSPaESPLEQLFGIDAETTIRCSNCGH 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   229 ESKLVSKFYELELN------IQGHKQLTDCISEFLKE--ERlEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFV 300
Cdd:pfam13423  148 ESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILKSslER-ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTN 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   301 FD-RQTGHKKKlnayiGFSESLDMEPYVEHKG--GSFVYELSAVLIHRGVSAYSGHYIAHVK-------DPQSGEWYKFN 370
Cdd:pfam13423  227 EEwRQLWKTPG-----WLPPEIGLTLSDDLQGdnEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFN 301


                   .
gi 114053325   371 D 371
Cdd:pfam13423  302 D 302
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 90-417 2.65e-19

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 88.19  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQvwflnlelrqALYLCPStcsdytkgdgihggkdyepqtICEHLQylfallqnsnrRYIdpsgfv 169
Cdd:cd02662     1 GLVNLGNTCFMNSVLQ----------ALASLPS---------------------LIEYLE-----------EFL------ 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 kalgldtgQQQDAQEFSKLFMSLLEdtlSKQKNPdvrnvvqqqFCGEYAYVTVCNQCGRESKL-VSKFYELELNIQGHKQ 248
Cdd:cd02662    33 --------EQQDAHELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKVrYESFTMLSLPVPNQSS 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  249 -----LTDCISEFLKEERLEGdnrYFCENCQSKqnatrkirLLSLPCTLNLQLMRFVFDRQtGHKKKLNAYIGFSESLDm 323
Cdd:cd02662    93 gsgttLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGR-GTSTKNSCKVSFPERLP- 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  324 epyvehkggSFVYELSAVLIHRGvSAYSGHYIAH------VKDPQSGE--------------WYKFNDEDIEKMEgkklq 383
Cdd:cd02662   160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfSKDKEPGSfvrmregpsstshpWWRISDTTVKEVS----- 224

                         330       340       350
                  ....*....|....*....|....*....|....
gi 114053325  384 lgiEEDLEPSKSqtrkpkcgkgthcsrnAYMLVY 417
Cdd:cd02662   225 ---ESEVLEQKS----------------AYMLFY 239
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
90-377 1.15e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 87.55  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   90 GLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKgDGIhgGKDYEPQTICEHLqYLFALLQNSNRRYIDPSGfv 169
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLK-NVI--RKPEPDLNQEEAL-KLFTALWSSKEHKVGWIP-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  170 kalglDTGQQQDAQEFsklfMSLLEDTLskqKNPDVRnvvqqqfCGEYAYVTVCNQCGRESK------LVSKFYELELNI 243
Cdd:COG5533    75 -----PMGSQEDAHEL----LGKLLDEL---KLDLVN-------SFTIRIFKTTKDKKKTSTgdwfdiIIELPDQTWVNN 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  244 QghKQLTDCIS---EFLKEERL--EGDNRYfcENCQSKQNATRKIRllSLPCTLNLQLMRFVFDrqtGHKKKLNAYIGfs 318
Cdd:COG5533   136 L--KTLQEFIDnmeELVDDETGvkAKENEE--LEVQAKQEYEVSFV--KLPKILTIQLKRFANL---GGNQKIDTEVD-- 204

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114053325  319 ESLDMEPYVEHKGG---SFVYELSAVLIHRGvSAYSGHYIAHVKdpQSGEWYKFNDEDIEKM 377
Cdd:COG5533   205 EKFELPVKHDQILNivkETYYDLVGFVLHQG-SLEGGHYIAYVK--KGGKWEKANDSDVTPV 263
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
249-376 4.04e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 89.94  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  249 LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTghKKKLNAYIGFS-ESLDMEPYV 327
Cdd:COG5560   677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE 754

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 114053325  328 EHKGGS-FVYELSAVLIHRGVSAySGHYIAHVKDPQSGEWYKFNDEDIEK 376
Cdd:COG5560   755 YMVDDPrLIYDLYAVDNHYGGLS-GGHYTAYARNFANNGWYLFDDSRITE 803
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 89-375 2.17e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 78.69  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   89 VGLTNLGATCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKgDGIH----GGKDYEP------QTICEHLQYLFALLQNS 158
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELAS-DYPTerriGGREVSRselqrsNQFVYELRSLFNDLIHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  159 NRRYIDPSGFVKALGLDtgqQQDAQEF---------SKLFMSLLEDTLSKQKN-PDVRNVVQQQFCGEY----AYVTVCN 224
Cdd:cd02666    81 NTRSVTPSKELAYLALR---QQDVTECidnvlfqleVALEPISNAFAGPDTEDdKEQSDLIKRLFSGKTkqqlVPESMGN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  225 QCGRESK-------LV-SKFYELELNIQGHKQ-LTDCISEFLKEERLEGDNRYFCENCQSKQNATRKI---------RLL 286
Cdd:cd02666   158 QPSVRTKterflslLVdVGKKGREIVVLLEPKdLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryelpSSI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  287 SLPCTLNLQLMRFVFDRQTGHKKKLNAYigfseSLDMEPYVEHKGgSFVYELSAVLIHRGvSAYSGHYIAHVKDPQSGEW 366
Cdd:cd02666   238 DDIDELIREAIQSESSLVRQAQNELAEL-----KHEIEKQFDDLK-SYGYRLHAVFIHRG-EASSGHYWVYIKDFEENVW 310


                  ....*....
gi 114053325  367 YKFNDEDIE 375
Cdd:cd02666   311 RKYNDETVT 319
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 178-417 2.21e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 70.66  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  178 QQQDAQEFSKLFMSLLEDTL----------SKQKNPDVrnvvqQQFCGEYAYVTVCNqcGRESKLVSKFYELELNIQGHK 247
Cdd:cd02665    21 QQQDVSEFTHLLLDWLEDAFqaaaeaispgEKSKNPMV-----QLFYGTFLTEGVLE--GKPFCNCETFGQYPLQVNGYG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  248 QLTDCISEFLKEERLEGDnryfcENCQSKQNATRKIrLLSLPCTLNLQLMRFVFDRqtGHKKKLNAYIGFSESLDMEPYv 327
Cdd:cd02665    94 NLHECLEAAMFEGEVELL-----PSDHSVKSGQERW-FTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQQVPY- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  328 ehkggsfvyELSAVLIHRGvSAYSGHYIAHVKDPQSGEWYKFNDEDIEKMEGKKlqlgIEEDlepsksqtrkpkcGKGTH 407
Cdd:cd02665   165 ---------ELHAVLVHEG-QANAGHYWAYIYKQSRQEWEKYNDISVTESSWEE----VERD-------------SFGGG 217

                         250
                  ....*....|
gi 114053325  408 CSRNAYMLVY 417
Cdd:cd02665   218 RNPSAYCLMY 227
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 173-374 3.29e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 61.78  E-value: 3.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  173 GLDTGQQQDAQEFSKLFMSLLEDTL---SKQKNPDVRNVVQQQFCGEYAYVT----VCNQCGRESKLVSKFYELELNIQG 245
Cdd:cd02673    27 EFDNDDQQDAHEFLLTLLEAIDDIMqvnRTNVPPSNIEIKRLNPLEAFKYTIessyVCIGCSFEENVSDVGNFLDVSMID 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  246 HK--QLTDCISEFLKEERLEGDnryfCENCqSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIgfsesldM 323
Cdd:cd02673   107 NKldIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEI-------M 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 114053325  324 EPYvEHKGGSfvYELSAVLIHRGVSAYSGHYIAHVKDPQSG-EWYKFNDEDI 374
Cdd:cd02673   175 KKY-CGTDAK--YSLVAVICHLGESPYDGHYIAYTKELYNGsSWLYCSDDEI 223
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 483-553 9.04e-10

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 56.22  E-value: 9.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114053325   483 EPYEFVSLEWLQKWL----DESTPTKPIDNN--ACLCSHDKLHPDKISIMK--RISEYAANIFYSRYGGGPRLTVKALC 553
Cdd:pfam06337    2 DKVYLISSKWLNKWKsyvkEPNNEPGPIDNSdlLDDESNGQLKPNLQEGVDyvIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 86-378 2.22e-07

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 54.63  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   86 NSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgihgGKDYEPQ-TICEHLQYLFALLQ----NSN- 159
Cdd:cd02669   117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL----------------YENYENIkDRKSELVKRLSELIrkiwNPRn 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  160 -RRYIDPSGFVKALGLDTGQ--QQDAQEFSKLFMSLLEDTLSKQ---KNPDVRNVVQQQFCGE-----YAYVTVCNQCGR 228
Cdd:cd02669   181 fKGHVSPHELLQAVSKVSKKkfSITEQSDPVEFLSWLLNTLHKDlggSKKPNSSIIHDCFQGKvqietQKIKPHAEEEGS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  229 ESKL----------VSKFYELELNIQG-----HKQLTDCISEFLKEERLegdNRYFCENCQSKQNATRKIRLLSLPCTLN 293
Cdd:cd02669   261 KDKFfkdsrvkktsVSPFLLLTLDLPPpplfkDGNEENIIPQVPLKQLL---KKYDGKTETELKDSLKRYLISRLPKYLI 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  294 LQLMRFvfDRQTGHKKKLNAYIGFS-ESLDMEPYVE---HKGGSFV-YELSAVLIHRGVSAYSGHYIAHVKDPQSGEWYK 368
Cdd:cd02669   338 FHIKRF--SKNNFFKEKNPTIVNFPiKNLDLSDYVHfdkPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFE 415

                         330
                  ....*....|
gi 114053325  369 FNDEDIEKME 378
Cdd:cd02669   416 IQDLNVKEVL 425
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 966-1019 1.30e-06

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 46.82  E-value: 1.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 114053325  966 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1019
Cdd:cd17039    15 VDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK-TLSDYGIKDGSTIHL 67
DUSP smart00695
Domain in ubiquitin-specific proteases;
482-555 9.83e-06

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 45.04  E-value: 9.83e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325    482 AEPYEFVSLEWLQKWLD-----ESTPTKPIDNNACLCSHD--KLHPDKI--SIMKRISEYAANIFYSRYGGGPR-LTVKA 551
Cdd:smart00695    5 GLTWYLISTRWYRQWADfvegkDGKDPGPIDNSGILCSHGgpRLKEHLVegEDYVLIPEELWNKLVRWYGGGPGpIPRKV 84


                    ....
gi 114053325    552 LCKD 555
Cdd:smart00695   85 VCQG 88
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 961-1019 1.14e-05

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 44.17  E-value: 1.14e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 114053325    961 EKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCaTLGTLGVIPESVILL 1019
Cdd:smart00213   12 TITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR-TLADYGIQDGSTIHL 69
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 75-371 6.71e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 45.97  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325   75 IDDPNCERRKKNSFVGLTNLGATCYVNTFLQVWFLNLELRQALYLcpstcsdytkgdgIHGGKDYEPQTICEhLQYLF-A 153
Cdd:cd02672     2 TEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAI-------------ILVACPKESCLLCE-LGYLFsT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  154 LLQNSNRRYIDPSGFvKALGLDTGQQQDAQEFSKLF-MSLLEDTLSKQKNPDVRNVVQQQFCGEYAyvtvcNQCGRESKL 232
Cdd:cd02672    68 LIQNFTRFLLETISQ-DQLGTPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKV-----TKAWCDTCC 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114053325  233 VSKFYELELNIQGhkqLTDCiseflkeerlegDNRYFCENCqSKQNATRKIRLLSLPCTLNLQlmrfvfdrqtghkkklN 312
Cdd:cd02672   142 KYQPLEQTTSIRH---LPDI------------LLLVLVINL-SVTNGEFDDINVVLPSGKVMQ----------------N 189

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114053325  313 AYIGFSESLDMEPYVEHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQ----SGEWYKFND 371
Cdd:cd02672   190 KVSPKAIDHDKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVFVIKVNeestHGRWYLFND 252
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 966-1019 1.23e-03

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 38.31  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 114053325   966 VSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDcATLGTLGVIPESVILL 1019
Cdd:pfam00240   15 VDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDD-QTLGEYGIEDGSTIHL 67
Ubl_AtNPL4_like cd17055
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ...
 954-1011 6.02e-03

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.


Pssm-ID: 340575  Cd Length: 73  Bit Score: 36.42  E-value: 6.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114053325  954 RHRKvrGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGK---ILNDDCATLGTLGV 1011
Cdd:cd17055     6 RSRD--GTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLSLDPGpdlLTAKSSATLSQLGL 64
 
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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