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Conserved domains on  [gi|747103219|ref|XP_011099795|]
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ubiquitin carboxyl-terminal hydrolase 26 isoform X1 [Sesamum indicum]

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 ...
 110-456 1.64e-126

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: 389.09  E-value: 1.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGE------------PVLNNLLRLFAQLHSSKMAFVDSAPFIQT 177
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELknmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  178 LELDNGVKQDSHEFLTLLFSLLERCLSQSKVPKARTIVQDLFRGGVSHVTRCSKCGNESeasSKIEDFYELELNVKGLKS 257
Cdd:cd02668    81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRES---SLPSKFYELELQLKGHKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  258 LDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPGELNMARRLS 337
Cdd:cd02668   158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  338 DCSELDYIYDLAAVLIHKGSAVNSGHYTAHIKDENSGEWWEFDDEHVSNLGRQPFGSTVSTPAAKggqngpvdcpsstkq 417
Cdd:cd02668   238 ESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAK--------------- 302

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 747103219  418 vdlvvegnhvdtnVLQSSDSNGvnhvqTFSSSDAYMLMY 456
Cdd:cd02668   303 -------------PRKSEIKKG-----THSSRTAYMLVY 323
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 976-1084 7.20e-24

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: 96.97  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  976 RRTSKRSKKatygnsvnLNVSGSTSIYQLKMMIWESFGVVKENQVLHKGPNIIDGETACLADVNIFPGDILWVTDSKIHE 1055
Cdd:cd01795     1 RRVRGERKS--------LTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPD 72

                          90       100
                  ....*....|....*....|....*....
gi 747103219 1056 NRDIADELLDPNldLQKAEEGFRGTLLAS 1084
Cdd:cd01795    73 DPDDADEADVSR--ARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 544-614 2.48e-09

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: 55.07  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   544 EKPYFWISTEWLRQWADSV-----TPLTIDNTSIQCFHGKVP-----VSKINYMkRLSAEAWTALTSKYDGGPTLAKDAY 613
Cdd:pfam06337    1 GDKVYLISSKWLNKWKSYVkepnnEPGPIDNSDLLDDESNGQlkpnlQEGVDYV-IVPEEVWEFLVEWYGGGPEIKRNVV 79


                   .
gi 747103219   614 C 614
Cdd:pfam06337   80 N 80
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 656-716 2.54e-08

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: 51.98  E-value: 2.54e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747103219   656 YYISKSWLQQWLRRKNidlPCDADSGP--TASL--RCPHGELMPELAPGAKRVLVPETLWDFIHQ 716
Cdd:pfam06337    5 YLISSKWLNKWKSYVK---EPNNEPGPidNSDLldDESNGQLKPNLQEGVDYVIVPEEVWEFLVE 66
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 783-871 3.12e-04

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: 40.43  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   783 KYYLLPSSWLAKWRSYVNSSGKNAYSADLDTLnavvdvLLCEKHCKLLekpPELVWKRELIfqksattggltLIAEDDWR 862
Cdd:pfam06337    3 KVYLISSKWLNKWKSYVKEPNNEPGPIDNSDL------LDDESNGQLK---PNLQEGVDYV-----------IVPEEVWE 62


                   ....*....
gi 747103219   863 LLCEEWGGT 871
Cdd:pfam06337   63 FLVEWYGGG 71
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-456 1.64e-126

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: 389.09  E-value: 1.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGE------------PVLNNLLRLFAQLHSSKMAFVDSAPFIQT 177
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELknmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  178 LELDNGVKQDSHEFLTLLFSLLERCLSQSKVPKARTIVQDLFRGGVSHVTRCSKCGNESeasSKIEDFYELELNVKGLKS 257
Cdd:cd02668    81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRES---SLPSKFYELELQLKGHKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  258 LDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPGELNMARRLS 337
Cdd:cd02668   158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  338 DCSELDYIYDLAAVLIHKGSAVNSGHYTAHIKDENSGEWWEFDDEHVSNLGRQPFGSTVSTPAAKggqngpvdcpsstkq 417
Cdd:cd02668   238 ESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAK--------------- 302

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 747103219  418 vdlvvegnhvdtnVLQSSDSNGvnhvqTFSSSDAYMLMY 456
Cdd:cd02668   303 -------------PRKSEIKKG-----THSSRTAYMLVY 323
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
109-401 1.83e-63

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 218.08  E-value: 1.83e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   109 AGLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGEP-----VLNNLLRLFAQL-HSSKMAFVDSAPFIQTL---- 178
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYnkdinLLCALRDLFKALqKNSKSSSVSPKMFKKSLgkln 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   179 -ELDNGVKQDSHEFLTLLFSLLERCLSQSKVPKARTIVQDLFRGGVSHVTRCSKCGNESEASskiEDFYELELNVKGLKS 257
Cdd:pfam00443   81 pDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETF---EPFSDLSLPIPGDSA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   258 ------LDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRcvFLPNTTTKKKITSVFSFPGELN 331
Cdd:pfam00443  158 elktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR--FSYNRSTWEKLNTEVEFPLELD 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747103219   332 M----ARRLSDCSELDYIYDLAAVLIHKGSaVNSGHYTAHIKDENSGEWWEFDDEHVSnlgRQPFGSTVSTPAA 401
Cdd:pfam00443  236 LsrylAEELKPKTNNLQDYRLVAVVVHSGS-LSSGHYIAYIKAYENNRWYKFDDEKVT---EVDEETAVLSSSA 305
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 110-388 1.48e-45

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 178.91  E-value: 1.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGEPVLNNLL-RLFAQLHSSKMAfVDSAPFIQTL---ELDNGVK 185
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALqRLFYNLQTGEEP-VDTTELTRSFgwdSDDSFMQ 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  186 QDSHEFLTLLFSLLERCLSQSKVPKArtiVQDLFrggVSHVTRCSKCGNESEASSKIEDFYELELNVKGLKSLDESLDDY 265
Cdd:COG5077   274 HDIQEFNRVLQDNLEKSMRGTVVENA---LNGIF---VGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRY 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  266 LSIEELQGDNQYYCDACATrVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPGELNMARRLSDCS----E 341
Cdd:COG5077   348 IQVETLDGDNRYNAEKHGL-QDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDAdkseN 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 747103219  342 LDYIYDLAAVLIHKGSaVNSGHYTAHIKDENSGEWWEFDDEHVSNLG 388
Cdd:COG5077   427 SDAVYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRAT 472
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 976-1084 7.20e-24

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: 96.97  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  976 RRTSKRSKKatygnsvnLNVSGSTSIYQLKMMIWESFGVVKENQVLHKGPNIIDGETACLADVNIFPGDILWVTDSKIHE 1055
Cdd:cd01795     1 RRVRGERKS--------LTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPD 72

                          90       100
                  ....*....|....*....|....*....
gi 747103219 1056 NRDIADELLDPNldLQKAEEGFRGTLLAS 1084
Cdd:cd01795    73 DPDDADEADVSR--ARVPEEGFKGTALLG 99
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 544-614 2.48e-09

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: 55.07  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   544 EKPYFWISTEWLRQWADSV-----TPLTIDNTSIQCFHGKVP-----VSKINYMkRLSAEAWTALTSKYDGGPTLAKDAY 613
Cdd:pfam06337    1 GDKVYLISSKWLNKWKSYVkepnnEPGPIDNSDLLDDESNGQlkpnlQEGVDYV-IVPEEVWEFLVEWYGGGPEIKRNVV 79


                   .
gi 747103219   614 C 614
Cdd:pfam06337   80 N 80
DUSP smart00695
Domain in ubiquitin-specific proteases;
541-607 4.32e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 4.32e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747103219    541 LSLEKPYFWISTEWLRQWADSV------TPLTIDNTSIQCFHG----KVPVSKINYMKRLSAEAWTALTSKYDGGPT 607
Cdd:smart00695    2 LEEGLTWYLISTRWYRQWADFVegkdgkDPGPIDNSGILCSHGgprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 656-716 2.54e-08

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: 51.98  E-value: 2.54e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747103219   656 YYISKSWLQQWLRRKNidlPCDADSGP--TASL--RCPHGELMPELAPGAKRVLVPETLWDFIHQ 716
Cdd:pfam06337    5 YLISSKWLNKWKSYVK---EPNNEPGPidNSDLldDESNGQLKPNLQEGVDYVIVPEEVWEFLVE 66
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 783-871 3.12e-04

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: 40.43  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   783 KYYLLPSSWLAKWRSYVNSSGKNAYSADLDTLnavvdvLLCEKHCKLLekpPELVWKRELIfqksattggltLIAEDDWR 862
Cdd:pfam06337    3 KVYLISSKWLNKWKSYVKEPNNEPGPIDNSDL------LDDESNGQLK---PNLQEGVDYV-----------IVPEEVWE 62


                   ....*....
gi 747103219   863 LLCEEWGGT 871
Cdd:pfam06337   63 FLVEWYGGG 71
DUSP smart00695
Domain in ubiquitin-specific proteases;
656-715 3.16e-03

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 37.72  E-value: 3.16e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747103219    656 YYISKSWLQQWLRRKNIDLPcdADSGP--TASLRCPHG--ELMPELAPGAKRVLVPETLWDFIH 715
Cdd:smart00695    9 YLISTRWYRQWADFVEGKDG--KDPGPidNSGILCSHGgpRLKEHLVEGEDYVLIPEELWNKLV 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 988-1046 6.08e-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: 36.38  E-value: 6.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   988 GNSVNLNVSGSTSIYQLKMMIWESFGVVKENQVL-HKGPNIIDGETacLADVNIFPGDIL 1046
Cdd:pfam00240    8 GKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLiYSGKVLEDDQT--LGEYGIEDGSTI 65
 
Name Accession Description Interval E-value
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-456 1.64e-126

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: 389.09  E-value: 1.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGE------------PVLNNLLRLFAQLHSSKMAFVDSAPFIQT 177
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELknmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  178 LELDNGVKQDSHEFLTLLFSLLERCLSQSKVPKARTIVQDLFRGGVSHVTRCSKCGNESeasSKIEDFYELELNVKGLKS 257
Cdd:cd02668    81 LGLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRES---SLPSKFYELELQLKGHKT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  258 LDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPGELNMARRLS 337
Cdd:cd02668   158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  338 DCSELDYIYDLAAVLIHKGSAVNSGHYTAHIKDENSGEWWEFDDEHVSNLGRQPFGSTVSTPAAKggqngpvdcpsstkq 417
Cdd:cd02668   238 ESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAK--------------- 302

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 747103219  418 vdlvvegnhvdtnVLQSSDSNGvnhvqTFSSSDAYMLMY 456
Cdd:cd02668   303 -------------PRKSEIKKG-----THSSRTAYMLVY 323
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-385 1.47e-74

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: 249.87  E-value: 1.47e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLG----GEPVLNNLLRLFAQLHSSKMAFVDSAPFIQTL---ELDN 182
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDddnkSVPLALQRLFLFLQLSESPVKTTELTDKTRSFgwdSLNT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  183 GVKQDSHEFLTLLFSLLERCLSQSKVPKartIVQDLFRGGVSHVTRCSKCGNESEassKIEDFYELELNVKGLKSLDESL 262
Cdd:cd02659    84 FEQHDVQEFFRVLFDKLEEKLKGTGQEG---LIKNLFGGKLVNYIICKECPHESE---REEYFLDLQVAVKGKKNLEESL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  263 DDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPGELNMAR-------R 335
Cdd:cd02659   158 DAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPytekglaK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 747103219  336 LSDCSELD----YIYDLAAVLIHKGSAvNSGHYTAHIKDENSGEWWEFDDEHVS 385
Cdd:cd02659   238 KEGDSEKKdsesYIYELHGVLVHSGDA-HGGHYYSYIKDRDDGKWYKFNDDVVT 290
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
109-401 1.83e-63

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 218.08  E-value: 1.83e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   109 AGLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGEP-----VLNNLLRLFAQL-HSSKMAFVDSAPFIQTL---- 178
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYnkdinLLCALRDLFKALqKNSKSSSVSPKMFKKSLgkln 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   179 -ELDNGVKQDSHEFLTLLFSLLERCLSQSKVPKARTIVQDLFRGGVSHVTRCSKCGNESEASskiEDFYELELNVKGLKS 257
Cdd:pfam00443   81 pDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETF---EPFSDLSLPIPGDSA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   258 ------LDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRcvFLPNTTTKKKITSVFSFPGELN 331
Cdd:pfam00443  158 elktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR--FSYNRSTWEKLNTEVEFPLELD 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747103219   332 M----ARRLSDCSELDYIYDLAAVLIHKGSaVNSGHYTAHIKDENSGEWWEFDDEHVSnlgRQPFGSTVSTPAA 401
Cdd:pfam00443  236 LsrylAEELKPKTNNLQDYRLVAVVVHSGS-LSSGHYIAYIKAYENNRWYKFDDEKVT---EVDEETAVLSSSA 305
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 110-385 2.32e-59

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: 204.25  E-value: 2.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNksfregvfsvepevlggepvlnnllrlfaqlhsskmafvdsapfiQtleldngvkQDSH 189
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFSE---------------------------------------------Q---------QDAH 26

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  190 EFLTLLFSLLERCLSQSKVP-----KARTIVQDLFRGGVSHVTRCSKCGNESEaSSKIEDFYELELNVKGL--KSLDESL 262
Cdd:cd02257    27 EFLLFLLDKLHEELKKSSKRtsdssSLKSLIHDLFGGKLESTIVCLECGHESV-STEPELFLSLPLPVKGLpqVSLEDCL 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  263 DDYLSIEELQGDNQYYCDaCATRVDATRSIKLRSLPAVLNFQLKRCVFLpNTTTKKKITSVFSFPGELNMARRL------ 336
Cdd:cd02257   106 EKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLsegekd 183

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 747103219  337 SDCSELDYIYDLAAVLIHKGSAVNSGHYTAHIKDENSGEWWEFDDEHVS 385
Cdd:cd02257   184 SDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVT 232
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 108-386 1.34e-46

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: 169.38  E-value: 1.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  108 PAGLTNLGATCYANSILQCLymnksfregvfsvepevLGGEPVLNNLLRLFAQLHSSKMAFV------------------ 169
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCL-----------------THTPPLANYLLSREHSKDCCNEGFCmmcaleahveralassgp 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  170 DSAPFIQTLELDN-------GVKQDSHEFLTLLFSLLERC----LSQSKVP----KARTIVQDLFRGGVSHVTRCSKCGN 234
Cdd:cd02661    64 GSAPRIFSSNLKQiskhfriGRQEDAHEFLRYLLDAMQKAcldrFKKLKAVdpssQETTLVQQIFGGYLRSQVKCLNCKH 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  235 ESEassKIEDFYELELNVKGLKSLDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRcvFLPNT 314
Cdd:cd02661   144 VSN---TYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKR--FSNFR 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747103219  315 TtkKKITSVFSFPGELNMARRLSDCSELDYIYDLAAVLIHKGSAVNSGHYTAHIKDENsGEWWEFDDEHVSN 386
Cdd:cd02661   219 G--GKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDDSKVSP 287
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 110-388 1.48e-45

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 178.91  E-value: 1.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGEPVLNNLL-RLFAQLHSSKMAfVDSAPFIQTL---ELDNGVK 185
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALqRLFYNLQTGEEP-VDTTELTRSFgwdSDDSFMQ 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  186 QDSHEFLTLLFSLLERCLSQSKVPKArtiVQDLFrggVSHVTRCSKCGNESEASSKIEDFYELELNVKGLKSLDESLDDY 265
Cdd:COG5077   274 HDIQEFNRVLQDNLEKSMRGTVVENA---LNGIF---VGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRY 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  266 LSIEELQGDNQYYCDACATrVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPGELNMARRLSDCS----E 341
Cdd:COG5077   348 IQVETLDGDNRYNAEKHGL-QDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDAdkseN 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 747103219  342 LDYIYDLAAVLIHKGSaVNSGHYTAHIKDENSGEWWEFDDEHVSNLG 388
Cdd:COG5077   427 SDAVYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRAT 472
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-385 5.34e-41

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: 153.23  E-value: 5.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMnksfregvfsvepevlggEPVLNNLLRLFAQLHSSKMAFVDSAP--FIQTL----EL-DN 182
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYF------------------ENLLTCLKDLFESISEQKKRTGVISPkkFITRLkrenELfDN 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  183 GVKQDSHEFLTLLFSLLERCL--------------SQSKVPKARTIVQDLFRGGVSHVTRCSKCGNeseASSKIEDFYEL 248
Cdd:cd02663    63 YMHQDAHEFLNFLLNEIAEILdaerkaekanrklnNNNNAEPQPTWVHEIFQGILTNETRCLTCET---VSSRDETFLDL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  249 ELNVKGLKSLDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFSFPG 328
Cdd:cd02663   140 SIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPL 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 747103219  329 ELNMARRLSDCSELDYIYDLAAVLIHKGSAVNSGHYTAHIKdeNSGEWWEFDDEHVS 385
Cdd:cd02663   220 ELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK--SHGGWLLFDDETVE 274
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-400 9.15e-39

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 144.35  E-value: 9.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLymnksfregvfsvepevlggepvlnnllrlFAQlhsskmafvdsapfiqtleldngvKQDSH 189
Cdd:cd02674     1 GLRNLGNTCYMNSILQCL------------------------------SAD------------------------QQDAQ 26

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  190 EFLTLLFSLLERclsqskvpkartIVQDLFRGGVSHVTRCSKCGNESeasSKIEDFYELELNVKGLK------SLDESLD 263
Cdd:cd02674    27 EFLLFLLDGLHS------------IIVDLFQGQLKSRLTCLTCGKTS---TTFEPFTYLSLPIPSGSgdapkvTLEDCLR 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  264 DYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRcvFLPNTTTKKKITSVFSFPGE-LNMARRLSD-CSE 341
Cdd:cd02674    92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR--FSFSRGSTRKLTTPVTFPLNdLDLTPYVDTrSFT 169

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 747103219  342 LDYIYDLAAVLIHKGSaVNSGHYTAHIKDENSGEWWEFDDEHVSnlgRQPFGSTVSTPA 400
Cdd:cd02674   170 GPFKYDLYAVVNHYGS-LNGGHYTAYCKNNETNDWYKFDDSRVT---KVSESSVVSSSA 224
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-385 1.60e-37

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 143.79  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGE-PVLNNLLRLFAQLHSSKMAFvdSAPFIQTLE------LDN 182
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSqSVMKKLQLLQAHLMHTQRRA--EAPPDYFLEasrppwFTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  183 GVKQDSHEFLTLLFSLLErclsqskvpkarTIVQDLFRGGVSHVTRCSKCGNESEassKIEDFYELELNVKGLKSLdesL 262
Cdd:cd02664    79 GSQQDCSEYLRYLLDRLH------------TLIEKMFGGKLSTTIRCLNCNSTSA---RTERFRDLDLSFPSVQDL---L 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  263 DDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKI----------------TSVFSF 326
Cdd:cd02664   141 NYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKImdnvsinevlslpvrvESKSSE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  327 PGELNMARRLSDCSELDYI---YDLAAVLIHKGSAVNSGHY---TAHIKD-----------------ENSGEWWEFDDEH 383
Cdd:cd02664   221 SPLEKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSESGHYftyARDQTDadstgqecpepkdaeenDESKNWYLFNDSR 300


                  ..
gi 747103219  384 VS 385
Cdd:cd02664   301 VT 302
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-385 4.85e-37

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 142.51  E-value: 4.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGEPVLNNLL-----RLFAQLHSSKmafvDSAPFIQT------- 177
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLscamdEIFQEFYYSG----DRSPYGPInllylsw 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  178 ---LELDNGVKQDSHEFLT-LLFSLLERCLSQ----SKVPKARTIVQDLFRGGVSHVTRCSKCGNESEASSKIEDFyELE 249
Cdd:cd02660    78 khsRNLAGYSQQDAHEFFQfLLDQLHTHYGGDkneaNDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL-SLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  250 LN-------------VKGLKSLDESLDDYLSIEELqGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRCVFLpNTTT 316
Cdd:cd02660   157 IPnkstpswalgesgVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKT 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747103219  317 KKKITSVFSFPGELNM---------ARRLSDCSELDYIYDLAAVLIHKGSaVNSGHYTAHIKDENsGEWWEFDDEHVS 385
Cdd:cd02660   235 SRKIDTYVQFPLELNMtpytsssigDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQGD-GQWFKFDDAMIT 310
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-385 8.52e-37

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 141.31  E-value: 8.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGGE----PVLNNLLRLFAQLHSSKMAFVDSApFIQTL------- 178
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANqssdNLTNALRDLFDTMDKKQEPVPPIE-FLQLLrmafpqf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  179 ---ELDNGVK-QDSHEFLTLLFSLLERCLSQSKvpKARTIVQDLFRGGVSHVTRCSkcGNESEASSKIEDFYELELNVKG 254
Cdd:cd02657    80 aekQNQGGYAqQDAEECWSQLLSVLSQKLPGAG--SKGSFIDQLFGIELETKMKCT--ESPDEEEVSTESEYKLQCHISI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  255 ---LKSLDESLDDYLS------IEELQGDNQYycdacatrvdaTRSIKLRSLPAVLNFQLKRCVFLPNTTTKKKITSVFS 325
Cdd:cd02657   156 tteVNYLQDGLKKGLEeeiekhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVK 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  326 FPGELNMARRLSDCSeldyIYDLAAVLIHKGSAVNSGHYTAHIKDENSGEWWEFDDEHVS 385
Cdd:cd02657   225 FPFELDLYELCTPSG----YYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVS 280
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-384 8.70e-29

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: 117.81  E-value: 8.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREGVFSVEPEVLGgEPVL--NNLLRLFAQLH--------SSKMAFVDSAPFIQtle 179
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPS-DVVDpaNDLNCQLIKLAdgllsgrySKPASLKSENDPYQ--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  180 ldNGVK--------------------QDSHEFLTLLFSLLERCLSQSKVPKartiVQDLFRGGVSHVTRCSKCGnesEAS 239
Cdd:cd02658    77 --VGIKpsmfkaligkghpefstmrqQDALEFLLHLIDKLDRESFKNLGLN----PNDLFKFMIEDRLECLSCK---KVK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  240 SKIEDFYELELNVKGLK--------------SLDESLDDYLSIEELQgdnqYYCDACATRVDATRSIKLRSLPAVLNFQL 305
Cdd:cd02658   148 YTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINM 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  306 KRCVFLPNTTTKKkiTSVFSF-PGELNMARrlsdcseldyiYDLAAVLIHKGSAVNSGHYTAHIK--DENSGEWWEFDDE 382
Cdd:cd02658   224 KRFQLLENWVPKK--LDVPIDvPEELGPGK-----------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDE 290


                  ..
gi 747103219  383 HV 384
Cdd:cd02658   291 KV 292
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-372 1.25e-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: 116.72  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFRegvfsvepEVLGGEPVLnnllrLFAQLHSSKMAFVDSapfiqtleldngVKQDSH 189
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALR--------ELLSETPKE-----LFSQVCRKAPQFKGY------------QQQDSH 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  190 EFLTLLFSLLerclsqskvpkaRTIVQDLFRGGVSHVTRCSKCGNeseASSKIEDFYELELNV----KGLKSLDESLDDY 265
Cdd:cd02667    56 ELLRYLLDGL------------RTFIDSIFGGELTSTIMCESCGT---VSLVYEPFLDLSLPRsdeiKSECSIESCLKQF 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  266 LSIEELQGDNQYYCDACatrVDATRSIKLRSLPAVLNFQLKRcVFLPNTTTKKKITSVFSFPGELNMA-----RRLSDCS 340
Cdd:cd02667   121 TEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKR-FQQPRSANLRKVSRHVSFPEILDLApfcdpKCNSSED 196

                         250       260       270
                  ....*....|....*....|....*....|..
gi 747103219  341 ELDYIYDLAAVLIHKGSaVNSGHYTAHIKDEN 372
Cdd:cd02667   197 KSSVLYRLYGVVEHSGT-MRSGHYVAYVKVRP 227
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 95-415 6.81e-24

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 104.20  E-value: 6.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   95 PDPSHDLRASSNTPAGLTNLGATCYANSILQCLYMNKSFREGV---FSVEPEVLGGEPVLNNLLRLFAQLHSSKMAfvds 171
Cdd:cd02671    11 SATSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLkhlVSLISSVEQLQSSFLLNPEKYNDELANQAP---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  172 APFIQTLELDNGV-----KQDSHEFLtllfslleRCLSQSkvpkARTIVQDLFRGGVSHVTRCSKCGNESE--------- 237
Cdd:cd02671    87 RRLLNALREVNPMyegylQHDAQEVL--------QCILGN----IQELVEKDFQGQLVLRTRCLECETFTErredfqdis 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  238 ------ASSKIEDFYELELNVKG-LKSLDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRcvF 310
Cdd:cd02671   155 vpvqesELSKSEESSEISPDPKTeMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKC--F 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  311 LPNTTTK------KKITSVFSFPGELNMaRRLSDCSELDyIYDLAAVLIHKGSAVNSGHYTAHIKdensgeWWEFDDEHV 384
Cdd:cd02671   233 AANGSEFdcygglSKVNTPLLTPLKLSL-EEWSTKPKND-VYRLFAVVMHSGATISSGHYTAYVR------WLLFDDSEV 304

                         330       340       350
                  ....*....|....*....|....*....|.
gi 747103219  385 SNLGRQPFGSTVStpaakggqngPVDCPSST 415
Cdd:cd02671   305 KVTEEKDFLEALS----------PNTSSTST 325
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
 976-1084 7.20e-24

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: 96.97  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  976 RRTSKRSKKatygnsvnLNVSGSTSIYQLKMMIWESFGVVKENQVLHKGPNIIDGETACLADVNIFPGDILWVTDSKIHE 1055
Cdd:cd01795     1 RRVRGERKS--------LTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSATLADLGILPGDVLYLKVDEPPD 72

                          90       100
                  ....*....|....*....|....*....
gi 747103219 1056 NRDIADELLDPNldLQKAEEGFRGTLLAS 1084
Cdd:cd01795    73 DPDDADEADVSR--ARVPEEGFKGTALLG 99
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
110-385 2.28e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 95.64  E-value: 2.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCL-YMNKSFRE--GVFSVEPEVL-----GGEPVLN--NLLRLFAQLHSSKMAFVDSAPfiqtle 179
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDEllDDLSKELKVLknvirKPEPDLNqeEALKLFTALWSSKEHKVGWIP------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  180 lDNGVKQDSHEFLTLLFSLLerclsqsKVPKARTIVQDLFrggvshvtrcsKCGNESEASSkIEDFYELEL------NVK 253
Cdd:COG5533    75 -PMGSQEDAHELLGKLLDEL-------KLDLVNSFTIRIF-----------KTTKDKKKTS-TGDWFDIIIelpdqtWVN 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  254 GLKSLDESLDdylsieelqGDNQYYCDACATRVDATRSIKLR----------SLPAVLNFQLKRCVflpNTTTKKKITSv 323
Cdd:COG5533   135 NLKTLQEFID---------NMEELVDDETGVKAKENEELEVQakqeyevsfvKLPKILTIQLKRFA---NLGGNQKIDT- 201

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747103219  324 fSFPGELNMARRLSDCSEL--DYIYDLAAVLIHKGSaVNSGHYTAHIKdeNSGEWWEFDDEHVS 385
Cdd:COG5533   202 -EVDEKFELPVKHDQILNIvkETYYDLVGFVLHQGS-LEGGHYIAYVK--KGGKWEKANDSDVT 261
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 110-385 1.27e-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: 89.35  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCLYMNKSFREgvfsvepevlggepVLNNLLrlfaqlhsskmafvdsapfiqtleldngVKQDSH 189
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIE--------------YLEEFL----------------------------EQQDAH 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  190 EFLTLLFSLLErclSQSKVPkartivqdlFRGGVSHVTRCSKCGNESEAssKIEDFYELELNVKGLK-----SLDESLDD 264
Cdd:cd02662    39 ELFQVLLETLE---QLLKFP---------FDGLLASRIVCLQCGESSKV--RYESFTMLSLPVPNQSsgsgtTLEHCLDD 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  265 YLSIEELQGdnqYYCDACATRVDAtrsiklrsLPAVLNFQLKRCVFLPNTTTKKKITSVfSFPGELNmarrlsdcselDY 344
Cdd:cd02662   105 FLSTEIIDD---YKCDRCQTVIVR--------LPQILCIHLSRSVFDGRGTSTKNSCKV-SFPERLP-----------KV 161

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747103219  345 IYDLAAVLIHKGSAvNSGHYTAH--------------------IKDENSGEWWEFDDEHVS 385
Cdd:cd02662   162 LYRLRAVVVHYGSH-SSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVK 221
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 108-385 8.70e-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: 77.15  E-value: 8.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  108 PAGLTNLGATCYANSILQCLYMNKSFREGVFSVEP-----------------------EVLGGEPVLNNLLRLFAQLHSS 164
Cdd:cd02666     1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDEskaelasdypterriggrevsrsELQRSNQFVYELRSLFNDLIHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  165 KMAFVDSAPFIQTLELDngvKQDSHEFLTLLFSLLERCLSQSKV----------PKARTIVQDLFRGGVSHVTRCSKCGN 234
Cdd:cd02666    81 NTRSVTPSKELAYLALR---QQDVTECIDNVLFQLEVALEPISNafagpdteddKEQSDLIKRLFSGKTKQQLVPESMGN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  235 ESEASSKIEDFYELELNV----------KGLKSLDESLD---DYLSIEELQGDNQYYCDACATR---VDATRSIKLRSLP 298
Cdd:cd02666   158 QPSVRTKTERFLSLLVDVgkkgreivvlLEPKDLYDALDryfDYDSLTKLPQRSQVQAQLAQPLqreLISMDRYELPSSI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  299 AVLNFQLKRCVflpnTTTKKKITSVFSFPGELNMARRLSDCSELDYIYDLAAVLIHKGSAvNSGHYTAHIKDENSGEWWE 378
Cdd:cd02666   238 DDIDELIREAI----QSESSLVRQAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRK 312


                  ....*..
gi 747103219  379 FDDEHVS 385
Cdd:cd02666   313 YNDETVT 319
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
257-384 1.75e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 78.39  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  257 SLDESLDDYLSIEELQGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLKRcvFLPNTTTKKKITSVFSFP-GELNMARR 335
Cdd:COG5560   676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPiDDLDLSGV 753

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 747103219  336 LSDCSELDYIYDLAAVLIHKGsAVNSGHYTAHIKDENSGEWWEFDDEHV 384
Cdd:COG5560   754 EYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRI 801
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 86-390 2.46e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 76.59  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   86 TSEIVNSLGPDP--SHDLRASSNTPA--GLTNLGATCYANSILQCLYMNKSFREgVFSVEPEVLGGEPVLNNLLRLFAQL 161
Cdd:cd02669    93 TKEQISDLDRDPklSRDLDGKPYLPGfvGLNNIKNNDYANVIIQALSHVKPIRN-FFLLYENYENIKDRKSELVKRLSEL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  162 ----HSSKmAF---VDSAPFIQTLEL------DNGVKQDSHEFLTLLFSLLERCLSQSKvPKARTIVQDLFRGGVSHVTR 228
Cdd:cd02669   172 irkiWNPR-NFkghVSPHELLQAVSKvskkkfSITEQSDPVEFLSWLLNTLHKDLGGSK-KPNSSIIHDCFQGKVQIETQ 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  229 csKCGNESEASSKIEDFYELELNVKGLK------SLD------------ESLDDYLSIEELQgdNQYYCDACATRVDATR 290
Cdd:cd02669   250 --KIKPHAEEEGSKDKFFKDSRVKKTSVspflllTLDlpppplfkdgneENIIPQVPLKQLL--KKYDGKTETELKDSLK 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  291 SIKLRSLPAVLNFQLKRcvFLPNTTTKKKITSVFSFPGELNMarrLSDCSELDYI-------YDLAAVLIHKGSAVNSGH 363
Cdd:cd02669   326 RYLISRLPKYLIFHIKR--FSKNNFFKEKNPTIVNFPIKNLD---LSDYVHFDKPslnlstkYNLVANIVHEGTPQEDGT 400

                         330       340
                  ....*....|....*....|....*..
gi 747103219  364 YTAHIKDENSGEWWEFDDEHVSNLGRQ 390
Cdd:cd02669   401 WRVQLRHKSTNKWFEIQDLNVKEVLPQ 427
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 185-401 6.48e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 72.21  E-value: 6.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  185 KQDSHEFLTLLFSLLERCL-----SQSKVPKARTIVQDLFRGGVSHVTRcskcgNESEASSKIEDFYELELNVKGLKSLD 259
Cdd:cd02665    22 QQDVSEFTHLLLDWLEDAFqaaaeAISPGEKSKNPMVQLFYGTFLTEGV-----LEGKPFCNCETFGQYPLQVNGYGNLH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  260 ESLDDYLSIEELQGDnqyycdACATRVDATRSIKLRSLPAVLNFQLKRCVFlpNTTTKKKITSVFSFPGELNMARrlsdc 339
Cdd:cd02665    97 ECLEAAMFEGEVELL------PSDHSVKSGQERWFTELPPVLTFELSRFEF--NQGRPEKIHDKLEFPQIIQQVP----- 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747103219  340 seldyiYDLAAVLIHKGSAvNSGHYTAHIKDENSGEWWEFDDEHV-----SNLGRQPFGsTVSTPAA 401
Cdd:cd02665   164 ------YELHAVLVHEGQA-NAGHYWAYIYKQSRQEWEKYNDISVtesswEEVERDSFG-GGRNPSA 222
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
109-381 5.25e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 64.98  E-value: 5.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   109 AGLTNLGATCYANSILQCLYMNKSFRE-GVFSVEPEVLGGEPVLNNLLRLFAQLHSSKMA------F---VDSAPFIQTL 178
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATECLKEHCLLCELGFLFDMLEKAKGKncqasnFlraLSSIPEASAL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   179 EL-DNGVKQDSHEFLTLL------FsLLERCLSQSKV-----PKARTIVQDLFRGGVSHVTRCSKCGNESEassKIEDFY 246
Cdd:pfam13423   81 GLlDEDRETNSAISLSSLiqsfnrF-LLDQLSSEENStppnpSPAESPLEQLFGIDAETTIRCSNCGHESV---RESSTH 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   247 ELELNVKGLKSLDESLDDYLSIEEL-------QGDNQYYCDACATRVDATRSIKLRSLPAVLNFQLkrCVFLPNTTTKKK 319
Cdd:pfam13423  157 VLDLIYPRKPSSNNKKPPNQTFSSIlksslerETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNA--ALTNEEWRQLWK 234

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   320 ITSvfSFPGELNMARRLSDCSELD-YIYDLAAVLIHKGSAVNSGHYTAHIK-------DENSGEWWEFDD 381
Cdd:pfam13423  235 TPG--WLPPEIGLTLSDDLQGDNEiVKYELRGVVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 544-614 2.48e-09

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: 55.07  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   544 EKPYFWISTEWLRQWADSV-----TPLTIDNTSIQCFHGKVP-----VSKINYMkRLSAEAWTALTSKYDGGPTLAKDAY 613
Cdd:pfam06337    1 GDKVYLISSKWLNKWKSYVkepnnEPGPIDNSDLLDDESNGQlkpnlQEGVDYV-IVPEEVWEFLVEWYGGGPEIKRNVV 79


                   .
gi 747103219   614 C 614
Cdd:pfam06337   80 N 80
DUSP smart00695
Domain in ubiquitin-specific proteases;
541-607 4.32e-09

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 54.29  E-value: 4.32e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747103219    541 LSLEKPYFWISTEWLRQWADSV------TPLTIDNTSIQCFHG----KVPVSKINYMKRLSAEAWTALTSKYDGGPT 607
Cdd:smart00695    2 LEEGLTWYLISTRWYRQWADFVegkdgkDPGPIDNSGILCSHGgprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 656-716 2.54e-08

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: 51.98  E-value: 2.54e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747103219   656 YYISKSWLQQWLRRKNidlPCDADSGP--TASL--RCPHGELMPELAPGAKRVLVPETLWDFIHQ 716
Cdd:pfam06337    5 YLISSKWLNKWKSYVK---EPNNEPGPidNSDLldDESNGQLKPNLQEGVDYVIVPEEVWEFLVE 66
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
110-250 5.41e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 50.65  E-value: 5.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  110 GLTNLGATCYANSILQCL---------YMNKSFREGVFSVEPEVLGGEpVLNNLLRLFAQLHSSKMAFVDSAPFIQTL-- 178
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLmhtwelrdyFLSDEYEESINEENPLGMHGS-VASAYADLIKQLYDGNLHAFTPSGFKKTIgs 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219  179 ---ELDNGVKQDSHEFLTLLFSLLERCLS------QSKVP-----------------------KARTIVQDLFRGGVSHV 226
Cdd:COG5560   346 fneEFSGYDQQDSQEFIAFLLDGLHEDLNriikkpYTSKPdlspgddvvvkkkakecwwehlkRNDSIITDLFQGMYKST 425

                         170       180
                  ....*....|....*....|....
gi 747103219  227 TRCSKCGNESEAsskIEDFYELEL 250
Cdd:COG5560   426 LTCPGCGSVSIT---FDPFMDLTL 446
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 783-871 3.12e-04

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: 40.43  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   783 KYYLLPSSWLAKWRSYVNSSGKNAYSADLDTLnavvdvLLCEKHCKLLekpPELVWKRELIfqksattggltLIAEDDWR 862
Cdd:pfam06337    3 KVYLISSKWLNKWKSYVKEPNNEPGPIDNSDL------LDDESNGQLK---PNLQEGVDYV-----------IVPEEVWE 62


                   ....*....
gi 747103219   863 LLCEEWGGT 871
Cdd:pfam06337   63 FLVEWYGGG 71
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 988-1048 1.92e-03

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: 37.96  E-value: 1.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747103219  988 GNSVNLNVSGSTSIYQLKMMIWESFGVVKENQVL-HKGPNIIDGETacLADVNIFPGDILWV 1048
Cdd:cd17039     8 GKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLiYNGKELKDDKT--LSDYGIKDGSTIHL 67
DUSP smart00695
Domain in ubiquitin-specific proteases;
656-715 3.16e-03

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 37.72  E-value: 3.16e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747103219    656 YYISKSWLQQWLRRKNIDLPcdADSGP--TASLRCPHG--ELMPELAPGAKRVLVPETLWDFIH 715
Cdd:smart00695    9 YLISTRWYRQWADFVEGKDG--KDPGPidNSGILCSHGgpRLKEHLVEGEDYVLIPEELWNKLV 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 988-1046 6.08e-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: 36.38  E-value: 6.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 747103219   988 GNSVNLNVSGSTSIYQLKMMIWESFGVVKENQVL-HKGPNIIDGETacLADVNIFPGDIL 1046
Cdd:pfam00240    8 GKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLiYSGKVLEDDQT--LGEYGIEDGSTI 65
 
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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