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Conserved domains on  [gi|564351991|ref|XP_006238573|]
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ubiquitin carboxyl-terminal hydrolase 24 isoform X1 [Rattus norvegicus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase 24( domain architecture ID 12996454)

ubiquitin carboxyl-terminal hydrolase 24 (UBP24) is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability

EC:  3.4.19.12
Gene Symbol:  USP24
Gene Ontology:  GO:0004843|GO:0016579
PubMed:  10603300

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1683-2040 4.69e-150

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: 469.43  E-value: 4.69e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1683 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1759
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1760 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1839
Cdd:cd02659    79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1840 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1919
Cdd:cd02659   159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1920 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 1999
Cdd:cd02659   239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 564351991 2000 LEYECFGGEYRPKVYDqtnPYPDVRRRYWNAYMLFYQRVSD 2040
Cdd:cd02659   297 AEEECFGGEETQKTYD---SGPRAFKRTTNAYMLFYERKSP 334
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 951-1029 4.59e-43

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.


:

Pssm-ID: 340585  Cd Length: 79  Bit Score: 152.08  E-value: 4.59e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351991  951 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 1029
Cdd:cd17065     1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
 6-42 1.61e-17

UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24, also called deubiquitinating enzyme 24, ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24, is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal peptidase C19 domain.


:

Pssm-ID: 270472  Cd Length: 37  Bit Score: 77.87  E-value: 1.61e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 564351991    6 EQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLT 42
Cdd:cd14286     1 EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT 37
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1683-2040 4.69e-150

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: 469.43  E-value: 4.69e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1683 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1759
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1760 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1839
Cdd:cd02659    79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1840 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1919
Cdd:cd02659   159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1920 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 1999
Cdd:cd02659   239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 564351991 2000 LEYECFGGEYRPKVYDqtnPYPDVRRRYWNAYMLFYQRVSD 2040
Cdd:cd02659   297 AEEECFGGEETQKTYD---SGPRAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1685-2035 9.00e-67

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 229.25  E-value: 9.00e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1685 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1759
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1760 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---REQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1830
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1831 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1910
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1911 YTVAGMArqdsssevgengrnmdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 1990
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 564351991  1991 EEFDLNDETLEyecfggeyrpkvydqtnpypdvrrryWNAYMLFY 2035
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 951-1029 4.59e-43

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.


Pssm-ID: 340585  Cd Length: 79  Bit Score: 152.08  E-value: 4.59e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351991  951 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 1029
Cdd:cd17065     1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1677-2137 7.21e-40

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 163.12  E-value: 7.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1677 DSRSISGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1756
Cdd:COG5077   186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1757 MWNKELYVReQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEI 1836
Cdd:COG5077   264 GWDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1837 SLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVA 1914
Cdd:COG5077   343 SFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1915 GMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFD 1994
Cdd:COG5077   420 DADKSENSDAV------------------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRVTRAT 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1995 LNdETLEyECFGGE--YRPKVYDQTNPypdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPSSPEI 2072
Cdd:COG5077   473 EK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVAAVDI 526

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564351991 2073 SPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2137
Cdd:COG5077   527 PPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
 6-42 1.61e-17

UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24, also called deubiquitinating enzyme 24, ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24, is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal peptidase C19 domain.


Pssm-ID: 270472  Cd Length: 37  Bit Score: 77.87  E-value: 1.61e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 564351991    6 EQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLT 42
Cdd:cd14286     1 EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT 37
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1683-2040 4.69e-150

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: 469.43  E-value: 4.69e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1683 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1759
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1760 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1839
Cdd:cd02659    79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1840 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1919
Cdd:cd02659   159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1920 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 1999
Cdd:cd02659   239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 564351991 2000 LEYECFGGEYRPKVYDqtnPYPDVRRRYWNAYMLFYQRVSD 2040
Cdd:cd02659   297 AEEECFGGEETQKTYD---SGPRAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1685-2035 9.00e-67

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 229.25  E-value: 9.00e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1685 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1759
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1760 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---REQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1830
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1831 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1910
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1911 YTVAGMArqdsssevgengrnmdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 1990
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 564351991  1991 EEFDLNDETLEyecfggeyrpkvydqtnpypdvrrryWNAYMLFY 2035
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 1686-2036 8.91e-60

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: 206.95  E-value: 8.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvr 1765
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1766 eQQDAYEFFTSLIDQMDEYLKKMGR--------EQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGV----TSCQS 1833
Cdd:cd02257    22 -QQDAHEFLLFLLDKLHEELKKSSKrtsdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVS 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1834 LEISLDQFVRGEVLEGSNAYYCEKCKeKRITVKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTV 1913
Cdd:cd02257   101 LEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLS 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1914 AGMARQDSSSEVGengrnmdqggggsprkkvalteNYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFNDTVIEE 1992
Cdd:cd02257   179 EGEKDSDSDNGSY----------------------KYELVAVVVHSGTsADSGHYVAYVKDP---SDGKWYKFNDDKVTE 233

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 564351991 1993 FDLNDETleyecfggeyrpkvydqtnpypDVRRRYWNAYMLFYQ 2036
Cdd:cd02257   234 VSEEEVL----------------------EFGSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2035 4.77e-49

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: 178.77  E-value: 4.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS-----------VFYQVQSLFGHLMESKLQYYVPENFWKI 1754
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepqtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1755 FkmwnkELYVREQQDAYEF---FTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSC 1831
Cdd:cd02668    81 L-----GLDTGQQQDAQEFsklFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1832 QSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPY 1911
Cdd:cd02668   156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1912 tvagMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRRgcgKGKWYKFNDTVI 1990
Cdd:cd02668   236 ----LAESDEGSYV------------------------YELSGVLIHQGVsAYSGHYIAHIKDEQ---TGEWYKFNDEDV 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564351991 1991 EE-----FDLNDETLEYECFGGEYRPKVYDQTnpypdvrrrywNAYMLFY 2035
Cdd:cd02668   285 EEmpgkpLKLGNSEDPAKPRKSEIKKGTHSSR-----------TAYMLVY 323
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2035 1.59e-44

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: 164.76  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS--VFYQVQSLFGHLMESKLQYYVPENFWKIFKMWNKELY 1763
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1764 VREQQDAYEFFTSLIDQM-----DEYLKKMGREQIFKNT------FQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ 1832
Cdd:cd02661    83 IGRQEDAHEFLRYLLDAMqkaclDRFKKLKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1833 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFdwesGRSIKYDEQIRFPWMLNMEPYt 1912
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQISFPETLDLSPY- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1913 vagmarqdsssevgengrnMDQGGGGSPRkkvaltenYELVGVIVHSG-QAHAGHYYSFIKDRRgcgkGKWYKFNDTVIE 1991
Cdd:cd02661   238 -------------------MSQPNDGPLK--------YKLYAVLVHSGfSPHSGHYYCYVKSSN----GKWYNMDDSKVS 286

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 564351991 1992 EFDLNDetleyecfggeyrpkVYDQtnpypdvrrrywNAYMLFY 2035
Cdd:cd02661   287 PVSIET---------------VLSQ------------KAYILFY 303
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 951-1029 4.59e-43

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.


Pssm-ID: 340585  Cd Length: 79  Bit Score: 152.08  E-value: 4.59e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351991  951 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 1029
Cdd:cd17065     1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2035 3.36e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 155.99  E-value: 3.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV--------------FYQVQSLFGHLMESKLQyyvpeNF 1751
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsclscamdeifqeFYYSGDRSPYGPINLLY-----LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1752 WKIfkmwNKELYVREQQDAYEFFTSLIDQM--------DEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMA 1823
Cdd:cd02660    77 WKH----SRNLAGYSQQDAHEFFQFLLDQLhthyggdkNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1824 LNL---------------GVTSCQSLEISLDQFVRGEVLeGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDw 1888
Cdd:cd02660   153 LSLdipnkstpswalgesGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1889 ESGRSIKYDEQIRFPWMLNMEPYTVAGMARQDSSSEVgengrnmdqggggSPRKKvaltenYELVGVIVHSGQAHAGHYY 1968
Cdd:cd02660   231 LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSL-------------DPDYT------YDLFAVVVHKGTLDTGHYT 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564351991 1969 SFIKDrrgcGKGKWYKFNDTVIEEFDLNDetleyecfggeyrpkVYDQtnpypdvrrrywNAYMLFY 2035
Cdd:cd02660   292 AYCRQ----GDGQWFKFDDAMITRVSEEE---------------VLKS------------QAYLLFY 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1677-2137 7.21e-40

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 163.12  E-value: 7.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1677 DSRSISGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1756
Cdd:COG5077   186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1757 MWNKELYVReQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEI 1836
Cdd:COG5077   264 GWDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1837 SLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVA 1914
Cdd:COG5077   343 SFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1915 GMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFD 1994
Cdd:COG5077   420 DADKSENSDAV------------------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRVTRAT 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1995 LNdETLEyECFGGE--YRPKVYDQTNPypdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPSSPEI 2072
Cdd:COG5077   473 EK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVAAVDI 526

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564351991 2073 SPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2137
Cdd:COG5077   527 PPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2036 1.16e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 144.76  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYmqpglpesllsvdddtdnpDDSVFYQVQSLFGHLMESKLQYYV--PENFWKIFKMWNKELY 1763
Cdd:cd02663     1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENELFD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1764 VREQQDAYEFFTSLIDQMDEYL---KKMGREQIFKNT--------------FQGIYSDQKICKDCPHRYEREEAFMALNL 1826
Cdd:cd02663    62 NYMHQDAHEFLNFLLNEIAEILdaeRKAEKANRKLNNnnnaepqptwvheiFQGILTNETRCLTCETVSSRDETFLDLSI 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1827 GVTSCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWML 1906
Cdd:cd02663   142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1907 NMEpytvagmarqdSSSEVGENGRNMdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDrrgcgKGKWYKF 1985
Cdd:cd02663   222 RLF-----------NTTDDAENPDRL-----------------YELVAVVVHIGGgPNHGHYVSIVKS-----HGGWLLF 268

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564351991 1986 NDTVIEEFDlnDETLEYecFggeyrpkVYDQTNPYpdvrrrywNAYMLFYQ 2036
Cdd:cd02663   269 DDETVEKID--ENAVEE--F-------FGDSPNQA--------TAYVLFYQ 300
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2036 1.66e-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 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: 138.96  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVfqqlymqpglpesllsvdddtdnpddsvfyqVQSLFGHlmesklqyyvpenfwkifkmwnkelyvr 1765
Cdd:cd02674     1 GLRNLGNTCYMNSI-------------------------------LQCLSAD---------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1766 eQQDAYEFFTSLIDQMDeylkkmgreQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNL------GVTSCQSLEISLD 1839
Cdd:cd02674    22 -QQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLpipsgsGDAPKVTLEDCLR 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1840 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPW-MLNMEPYtvagmar 1918
Cdd:cd02674    92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLnDLDLTPY------- 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1919 qdsssevgengrnMDQGGGGSPRKkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDE 1998
Cdd:cd02674   163 -------------VDTRSFTGPFK-------YDLYAVVNHYGSLNGGHYTAYCKNNE---TNDWYKFDDSRVTKVSESSV 219

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 564351991 1999 tleyecfggeyrpkvydQTNpypdvrrrywNAYMLFYQ 2036
Cdd:cd02674   220 -----------------VSS----------SAYILFYE 230
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-1997 2.78e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 138.78  E-value: 2.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENfwKIFK-MWNKELYV 1764
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD--YFLEaSRPPWFTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1765 REQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLeisLDQFVRG 1844
Cdd:cd02664    79 GSQQDCSEYLRYLLDRLHTLIEKM---------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL---LNYFLSP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1845 EVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIK------YDEQIRFPwmlnmepytvagMAR 1918
Cdd:cd02664   147 EKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKimdnvsINEVLSLP------------VRV 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1919 QDSSSEVGENGRNMDQGGGGSprkKVALTENYELVGVIVHSG-QAHAGHYYSF---IKDRRGCGK--------------G 1980
Cdd:cd02664   215 ESKSSESPLEKKEEESGDDGE---LVTRQVHYRLYAVVVHSGySSESGHYFTYardQTDADSTGQecpepkdaeendesK 291

                         330
                  ....*....|....*..
gi 564351991 1981 KWYKFNDTVIEEFDLND 1997
Cdd:cd02664   292 NWYLFNDSRVTFSSFES 308
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2036 3.40e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 119.41  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDtdnpddsvfyqvqsLFGHLMESKLQYyvpenfwKIFKmwnkelyvr 1765
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAPQF-------KGYQ--------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1766 eQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ----SLEISLDQF 1841
Cdd:cd02667    51 -QQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIksecSIESCLKQF 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1842 VRGEVLEGSNAYYCEKCKEKRitvKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYtvagMARQDS 1921
Cdd:cd02667   121 TEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPF----CDPKCN 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1922 SSEVGENGRnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDR------------------RGCGKGKWY 1983
Cdd:cd02667   193 SSEDKSSVL-------------------YRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeAGPGSGQWY 253

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564351991 1984 KFNDTVIEEFDLnDETLEYEcfggeyrpkvydqtnpypdvrrrywnAYMLFYQ 2036
Cdd:cd02667   254 YISDSDVREVSL-EEVLKSE--------------------------AYLLFYE 279
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2036 3.89e-26

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: 111.65  E-value: 3.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYmqpGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLmeSKL-------QYYVPENFW------ 1752
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLF---SIPSFQWRYDDLENKFPSDVVDPANDLNCQL--IKLadgllsgRYSKPASLKsendpy 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1753 ------KIFKM----WNKELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIysDQKI-CKDCPHRY--EREE 1819
Cdd:cd02658    76 qvgikpSMFKAligkGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMI--EDRLeCLSCKKVKytSELS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1820 AFMALNL------------GVTSCQSLEISLDQFVRGEVLEgsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGF- 1886
Cdd:cd02658   154 EILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLl 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1887 -DWesgRSIKYDEQIRFPWMLnmepytvagmarqdsssevgengrnmdqGGGgsprkkvalteNYELVGVIVHSG-QAHA 1964
Cdd:cd02658   230 eNW---VPKKLDVPIDVPEEL----------------------------GPG-----------KYELIAFISHKGtSVHS 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564351991 1965 GHYYSFIKdRRGCGKGKWYKFNDTvieefdlndetleyecfggeyrpKVYDQTNPyPDVRRrywNAYMLFYQ 2036
Cdd:cd02658   268 GHYVAHIK-KEIDGEGKWVLFNDE-----------------------KVVASQDP-PEMKK---LGYIYFYQ 311
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-1987 7.80e-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 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: 89.70  E-value: 7.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQV---QSLFGHlMESKLQYYVPENFWKIF------- 1755
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTnalRDLFDT-MDKKQEPVPPIEFLQLLrmafpqf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1756 -KMWNKELYvrEQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKI-CKDCPHRYE---REEAFMALNLGVTS 1830
Cdd:cd02657    80 aEKQNQGGY--AQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMkCTESPDEEEvstESEYKLQCHISITT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1831 -CQSLEISLDQFVRGEVLEGSnayycEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNME 1909
Cdd:cd02657   158 eVNYLQDGLKKGLEEEIEKHS-----PTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564351991 1910 PYtvagmarqdsssevgengrnmdqggggsprkkVALTENYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFND 1987
Cdd:cd02657   233 EL--------------------------------CTPSGYYELVAVITHQGRsADSGHYVAWVRRK---NDGKWIKFDD 276
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
 6-42 1.61e-17

UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24, also called deubiquitinating enzyme 24, ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24, is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal peptidase C19 domain.


Pssm-ID: 270472  Cd Length: 37  Bit Score: 77.87  E-value: 1.61e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 564351991    6 EQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLT 42
Cdd:cd14286     1 EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT 37
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2036 3.19e-17

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 83.57  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvR 1765
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------L 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1766 EQQDAYEFFTSLIDQMdeylkkmgrEQIFKNTFQGIYSDQKICKDCPHRYE-REEAFMALNLGV-----TSCQSLEISLD 1839
Cdd:cd02662    33 EQQDAHELFQVLLETL---------EQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVpnqssGSGTTLEHCLD 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1840 QFVRGEVLEGsnaYYCEKCKEKritvkrtcIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLnmepytvagmarq 1919
Cdd:cd02662   104 DFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERL------------- 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1920 dsssevgengrnmdqggggsPRKKvaltenYELVGVIVHSGQAHAGHYYSF-----------------IKDRRGCGKGKW 1982
Cdd:cd02662   159 --------------------PKVL------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrMREGPSSTSHPW 212

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564351991 1983 YKFNDTVIEEFDLNDETLEYEcfggeyrpkvydqtnpypdvrrrywnAYMLFYQ 2036
Cdd:cd02662   213 WRISDTTVKEVSESEVLEQKS--------------------------AYMLFYE 240
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1661-1994 8.73e-17

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 84.17  E-value: 8.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1661 QPDPALTKE-FDYLPPvdsrsisgFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDdsvfyQVQSLFGHLM 1739
Cdd:cd02671     8 QPSSATSCEkRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVE-----QLQSSFLLNP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1740 E---SKLQYYVPENFWKIFKMWNKELYVREQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYE 1816
Cdd:cd02671    75 EkynDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKD---------FQGQLVLRTRCLECETFTE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1817 REEAFMALNLGV------TSCQSLEISLD-------------QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVL 1877
Cdd:cd02671   146 RREDFQDISVPVqeselsKSEESSEISPDpktemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1878 VIHLMRFG-----FDWESGRSiKYDEQIRFPWMLNMEpytvagmarqdsssevgengrnmdqGGGGSPRKKValtenYEL 1952
Cdd:cd02671   226 TIHLKCFAangseFDCYGGLS-KVNTPLLTPLKLSLE-------------------------EWSTKPKNDV-----YRL 274

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 564351991 1953 VGVIVHSG-QAHAGHYYSFIkdrrgcgkgKWYKFNDT---VIEEFD 1994
Cdd:cd02671   275 FAVVMHSGaTISSGHYTAYV---------RWLLFDDSevkVTEEKD 311
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1685-1990 1.33e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 74.23  E-value: 1.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1685 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENFWKIFKMW--NKEL 1762
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeASAL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1763 ----YVREQQDAyEFFTSLI--------DQM-DEYLKKMGREQ----IFKNTFQGIYSDQKICKDCPHRYEREEAFMALN 1825
Cdd:pfam13423   81 glldEDRETNSA-ISLSSLIqsfnrfllDQLsSEENSTPPNPSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1826 L--------------GVTSCQSLEISLDQfvrgevlEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESG 1891
Cdd:pfam13423  160 LiyprkpssnnkkppNQTFSSILKSSLER-------ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991  1892 RSIKydeqirfPWmLNMEPYTVagmarqdsssevgengrnMDQGGGGSPRKKValtenYELVGVIVH-SGQAHAGHYYSF 1970
Cdd:pfam13423  233 WKTP-------GW-LPPEIGLT------------------LSDDLQGDNEIVK-----YELRGVVVHiGDSGTSGHLVSF 281

                          330       340
                   ....*....|....*....|....
gi 564351991  1971 IK----DRRGCGKGKWYKFNDTVI 1990
Cdd:pfam13423  282 VKvadsELEDPTESQWYLFNDFLV 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1833-2039 4.36e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 75.30  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1833 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRfgFDWESGRSIKYDEQIRFPWM-LNMEPY 1911
Cdd:COG5560   676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIDdLDLSGV 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1912 TVAGMarqdsSSEVGengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgCGKGKWYKFNDTVIE 1991
Cdd:COG5560   754 EYMVD-----DPRLI-----------------------YDLYAVDNHYGGLSGGHYTAYARN---FANNGWYLFDDSRIT 802

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 564351991 1992 EFDLNDETLEyecfggeyrpkvydqtnpypdvrrrywNAYMLFYQRVS 2039
Cdd:COG5560   803 EVDPEDSVTS---------------------------SAYVLFYRRKS 823
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1686-1987 2.50e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQL-YMQPGLPESLLsvdddTDNPDDSVFYQV-----QSLFGHLMESKLQYYVPENFWKIFKMWN 1759
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDELLD-----DLSKELKVLKNVirkpePDLNQEEALKLFTALWSSKEHKVGWIPP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1760 KElyvrEQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTfqgiysdqkicKDCPHRYEREeaFMALNLGVTSCQSLEIS-- 1837
Cdd:COG5533    76 MG----SQEDAHELLGKLLDELKLDLVNSFTIRIFKTT-----------KDKKKTSTGD--WFDIIIELPDQTWVNNLkt 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1838 LDQFvrgevLEGSNAYYCEKC-------KEKRITVKR---TCIKSLPSVLVIHLMRFGFDwesGRSIKYDEQIRfpwmln 1907
Cdd:COG5533   139 LQEF-----IDNMEELVDDETgvkakenEELEVQAKQeyeVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1908 mEPYTVAgmARQDSSSEVGENGRnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgcgKGKWYKFND 1987
Cdd:COG5533   205 -EKFELP--VKHDQILNIVKETY-------------------YDLVGFVLHQGSLEGGHYIAYVKK-----GGKWEKAND 257
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1686-2014 2.57e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 62.96  E-value: 2.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1686 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklQYYVPENFWKIFKmWnkelyvr 1765
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLFSQ-------------------------------------QQDVSEFTHLLLD-W------- 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1766 eQQDAYEFFTSLIDQMDEYLKKMgrEQIFKNTF--QGIYSDQKICKDcphryereEAFMALNLGVTSCQSLEISLD-QFV 1842
Cdd:cd02665    36 -LEDAFQAAAEAISPGEKSKNPM--VQLFYGTFltEGVLEGKPFCNC--------ETFGQYPLQVNGYGNLHECLEaAMF 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1843 RGEVlEGSNAYYCEKCKEKRITVKrtciksLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPWMLNMEPYtvagmarqdss 1922
Cdd:cd02665   105 EGEV-ELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQVPY----------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1923 sevgengrnmdqggggsprkkvaltenyELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLndETLEY 2002
Cdd:cd02665   165 ----------------------------ELHAVLVHEGQANAGHYWAYIYKQS---RQEWEKYNDISVTESSW--EEVER 211

                         330
                  ....*....|..
gi 564351991 2003 ECFGGEYRPKVY 2014
Cdd:cd02665   212 DSFGGGRNPSAY 223
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 958-1028 1.13e-07

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: 50.67  E-value: 1.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564351991  958 LNVTYESTKdTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLtvnKDQKLLHQLGFSDEQVLTV 1028
Cdd:cd17039     1 ITVKTLDGK-TYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKEL---KDDKTLSDYGIKDGSTIHL 67
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1766-2036 1.94e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 54.46  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1766 EQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKickdcphRYEREEAFMalnlgvtSCQSLEISLDQFVRGE 1845
Cdd:cd02670    22 EQQDPEEFFNFITDKLLMPLLEP---------KVDIIHGGK-------KDQDDDKLV-------NERLLQIPVPDDDDGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1846 VLEgsnayyCEKCKEKRITVKRtcIKSLPSVLVIHLMRFGfdWESGRSIKYDEQIRFPWMLNMePYTVAGMARQDS--SS 1923
Cdd:cd02670    79 GIT------LEQCLEQYFNNSV--FAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDI-PDFVADDPRACSkcQL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1924 EVGENGRNMDQGGGGSPRKKValtenyeLVGVIVHSGQA-HAGHYYSFIK--------DRRGCGKGKWYKFNDtvieefd 1994
Cdd:cd02670   148 ECRVCYDDKDFSPTCGKFKLS-------LCSAVCHRGTSlETGHYVAFVRygsyslteTDNEAYNAQWVFFDD------- 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 564351991 1995 LNDetleyecfggeyRPKVYDQTNpYPDVRRRYWnAYMLFYQ 2036
Cdd:cd02670   214 MAD------------RDGVSNGFN-IPAARLLED-PYMLFYQ 241
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1950-2000 3.32e-06

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 51.72  E-value: 3.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564351991 1950 YELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVIEEFDLNDETL 2000
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDF---EENVWRKYNDETVTVVPASEVFL 328
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1832-2003 5.52e-04

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 44.43  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1832 QSLEISLDQFVrgevlegSNAYYCEKCKEKRITVKRTCIKSLP----SVLVIHLMRFGfdweSGRSIKYDEQIRFPWMLN 1907
Cdd:cd02672   121 QLLKRSLDLEK-------VTKAWCDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTN----GEFDDINVVLPSGKVMQN 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1908 MEPYtvagmARQDSSSEVGENGRNMdqggggsprkkvalTENYELVGVIVH-SGQAHAGHYYSF-IKDRRGCGKGKWYKF 1985
Cdd:cd02672   190 KVSP-----KAIDHDKLVKNRGQES--------------IYKYELVGYVCEiNDSSRGQHNVVFvIKVNEESTHGRWYLF 250

                         170
                  ....*....|....*...
gi 564351991 1986 NDTVIEEFDLNDETLEYE 2003
Cdd:cd02672   251 NDFLVTPVSELAYILLYQ 268
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1683-1788 3.02e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 42.95  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1683 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS---VDDDTDNPDDSVFYQVQSLFGHLMES----KLQYYVPENFWKIF 1755
Cdd:COG5560   264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdeyEESINEENPLGMHGSVASAYADLIKQlydgNLHAFTPSGFKKTI 343

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564351991 1756 KMWNKELYVREQQDAYEFFTSLIDQMDEYLKKM 1788
Cdd:COG5560   344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI 376
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1645-1992 3.11e-03

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 42.69  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1645 PSNLQIITKELLSMHHQPDPALTKE----FDYLPPV-----DSRSISGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS 1715
Cdd:cd02669    71 PDNYEIIDSSLDDIKYVLNPTYTKEqisdLDRDPKLsrdldGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1716 V-DDDTDNPDDSVFYQVQS-LFGHLMESKL--QYYVPENFWKIFKMW-NKELYVREQQDAYEFFTSLIDQMDEYLKKMGR 1790
Cdd:cd02669   151 YeNYENIKDRKSELVKRLSeLIRKIWNPRNfkGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKK 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1791 --EQIFKNTFQG---IYSdQKIckdcPHRYEREEAFMALNLGVTSCQS-----LEISLD-----------------QFVR 1843
Cdd:cd02669   231 pnSSIIHDCFQGkvqIET-QKI----KPHAEEEGSKDKFFKDSRVKKTsvspfLLLTLDlpppplfkdgneeniipQVPL 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564351991 1844 GEVLEGsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFgfdwESGRSIKYDEQ--IRFPWMLNMEPYTVAGMARQDS 1921
Cdd:cd02669   306 KQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRF----SKNNFFKEKNPtiVNFPIKNLDLSDYVHFDKPSLN 378

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564351991 1922 SSevgengrnmdqggggsprkkvaltENYELVGVIVHSGQAH-AGHYYSFIKDRrgcGKGKWYKFNDTVIEE 1992
Cdd:cd02669   379 LS------------------------TKYNLVANIVHEGTPQeDGTWRVQLRHK---STNKWFEIQDLNVKE 423
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 11-41 4.33e-03

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 37.07  E-value: 4.33e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 564351991   11 TLLCMGFSdPATIRKALRLAKNDINEAVALL 41
Cdd:cd14297     6 QLVDMGFT-EAQARKALRKTNNNVERAVDWL 35
 
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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