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Conserved domains on  [gi|568929280|ref|XP_006503240|]
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ubiquitin carboxyl-terminal hydrolase 24 isoform X2 [Mus musculus]

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 ...
 1704-2061 1.12e-149

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: 468.28  E-value: 1.12e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1704 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1780
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1781 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1860
Cdd:cd02659    79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1861 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1940
Cdd:cd02659   159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1941 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2020
Cdd:cd02659   239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568929280 2021 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2061
Cdd:cd02659   297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 972-1050 3.81e-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: 152.46  E-value: 3.81e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929280  972 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 1050
Cdd:cd17065     1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
 6-42 1.50e-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: 1.50e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568929280    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 ...
 1704-2061 1.12e-149

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: 468.28  E-value: 1.12e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1704 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1780
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1781 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1860
Cdd:cd02659    79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1861 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1940
Cdd:cd02659   159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1941 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2020
Cdd:cd02659   239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568929280 2021 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2061
Cdd:cd02659   297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1706-2056 7.93e-67

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 229.25  E-value: 7.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1706 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1780
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1781 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---REQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1851
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1852 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1931
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1932 YTVAGMArqdsssevgengrnmdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 2011
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 568929280  2012 EEFDLNDETLEyecfggeyrpkvydqtnpytdvrrryWNAYMLFY 2056
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 972-1050 3.81e-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: 152.46  E-value: 3.81e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929280  972 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 1050
Cdd:cd17065     1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1698-2158 6.09e-40

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 163.12  E-value: 6.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1698 DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1777
Cdd:COG5077   186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1778 MWNKELYVReQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEI 1857
Cdd:COG5077   264 GWDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1858 SLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVA 1935
Cdd:COG5077   343 SFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1936 GMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFD 2015
Cdd:COG5077   420 DADKSENSDAV------------------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRVTRAT 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 2016 LNdETLEyECFGGE--YRPKVYDQTNPytdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPSSPEI 2093
Cdd:COG5077   473 EK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVAAVDI 526

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929280 2094 SPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2158
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 1.50e-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: 1.50e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568929280    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 ...
 1704-2061 1.12e-149

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: 468.28  E-value: 1.12e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1704 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1780
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1781 KELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1860
Cdd:cd02659    79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1861 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQ 1940
Cdd:cd02659   159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1941 DsssevgengrnmdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2020
Cdd:cd02659   239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568929280 2021 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2061
Cdd:cd02659   297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1706-2056 7.93e-67

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 229.25  E-value: 7.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1706 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1780
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1781 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---REQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1851
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1852 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1931
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1932 YTVAGMArqdsssevgengrnmdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 2011
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 568929280  2012 EEFDLNDETLEyecfggeyrpkvydqtnpytdvrrryWNAYMLFY 2056
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 1707-2057 7.12e-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: 207.34  E-value: 7.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvr 1786
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1787 eQQDAYEFFTSLIDQMDEYLKKMGR--------EQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGV----TSCQS 1854
Cdd:cd02257    22 -QQDAHEFLLFLLDKLHEELKKSSKrtsdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVS 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1855 LEISLDQFVRGEVLEGSNAYYCEKCKeKRITVKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTV 1934
Cdd:cd02257   101 LEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLS 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1935 AGMARQDSSSEVGengrnmdqggggsprkkvalteNYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFNDTVIEE 2013
Cdd:cd02257   179 EGEKDSDSDNGSY----------------------KYELVAVVVHSGTsADSGHYVAYVKDP---SDGKWYKFNDDKVTE 233

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 568929280 2014 FDLNDEtleyecfggeyrpkvydqtnpyTDVRRRYWNAYMLFYQ 2057
Cdd:cd02257   234 VSEEEV----------------------LEFGSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2056 4.68e-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: 4.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS-----------VFYQVQSLFGHLMESKLQYYVPENFWKI 1775
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepqtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1776 FkmwnkELYVREQQDAYEF---FTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSC 1852
Cdd:cd02668    81 L-----GLDTGQQQDAQEFsklFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1853 QSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPY 1932
Cdd:cd02668   156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1933 tvagMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRRgcgKGKWYKFNDTVI 2011
Cdd:cd02668   236 ----LAESDEGSYV------------------------YELSGVLIHQGVsAYSGHYIAHIKDEQ---TGEWYKFNDEDV 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568929280 2012 EE-----FDLNDETLEYECFGGEYRPKVYDQTnpytdvrrrywNAYMLFY 2056
Cdd:cd02668   285 EEmpgkpLKLGNSEDPAKPRKSEIKKGTHSSR-----------TAYMLVY 323
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2056 1.50e-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: 1.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS--VFYQVQSLFGHLMESKLQYYVPENFWKIFKMWNKELY 1784
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1785 VREQQDAYEFFTSLIDQM-----DEYLKKMGREQIFKNT------FQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ 1853
Cdd:cd02661    83 IGRQEDAHEFLRYLLDAMqkaclDRFKKLKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1854 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFdwesGRSIKYDEQIRFPWMLNMEPYt 1933
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQISFPETLDLSPY- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1934 vagmarqdsssevgengrnMDQGGGGSPRkkvaltenYELVGVIVHSG-QAHAGHYYSFIKDRRgcgkGKWYKFNDTVIE 2012
Cdd:cd02661   238 -------------------MSQPNDGPLK--------YKLYAVLVHSGfSPHSGHYYCYVKSSN----GKWYNMDDSKVS 286

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 568929280 2013 EFDLNDetleyecfggeyrpkVYDQtnpytdvrrrywNAYMLFY 2056
Cdd:cd02661   287 PVSIET---------------VLSQ------------KAYILFY 303
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
 972-1050 3.81e-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: 152.46  E-value: 3.81e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929280  972 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVK 1050
Cdd:cd17065     1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2056 3.05e-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: 3.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV--------------FYQVQSLFGHLMESKLQyyvpeNF 1772
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsclscamdeifqeFYYSGDRSPYGPINLLY-----LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1773 WKIfkmwNKELYVREQQDAYEFFTSLIDQM--------DEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMA 1844
Cdd:cd02660    77 WKH----SRNLAGYSQQDAHEFFQFLLDQLhthyggdkNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1845 LNL---------------GVTSCQSLEISLDQFVRGEVLeGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDw 1909
Cdd:cd02660   153 LSLdipnkstpswalgesGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1910 ESGRSIKYDEQIRFPWMLNMEPYTVAGMARQDSSSEVgengrnmdqggggSPRKKvaltenYELVGVIVHSGQAHAGHYY 1989
Cdd:cd02660   231 LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSL-------------DPDYT------YDLFAVVVHKGTLDTGHYT 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568929280 1990 SFIKDrrgcGKGKWYKFNDTVIEEFDLNDetleyecfggeyrpkVYDQtnpytdvrrrywNAYMLFY 2056
Cdd:cd02660   292 AYCRQ----GDGQWFKFDDAMITRVSEEE---------------VLKS------------QAYLLFY 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 1698-2158 6.09e-40

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 163.12  E-value: 6.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1698 DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1777
Cdd:COG5077   186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1778 MWNKELYVReQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEI 1857
Cdd:COG5077   264 GWDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1858 SLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVA 1935
Cdd:COG5077   343 SFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDR 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1936 GMARQDSSSEVgengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFD 2015
Cdd:COG5077   420 DADKSENSDAV------------------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRVTRAT 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 2016 LNdETLEyECFGGE--YRPKVYDQTNPytdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPSSPEI 2093
Cdd:COG5077   473 EK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVAAVDI 526

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568929280 2094 SPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2158
Cdd:COG5077   527 PPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2057 3.79e-38

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: 146.30  E-value: 3.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYmqpglpesllsvdddtdnpDDSVFYQVQSLFGHLMESKLQYYV--PENFWKIFKMWNKELY 1784
Cdd:cd02663     1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENELFD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1785 VREQQDAYEFFTSLIDQMDEYL---KKMGREQIFKNT--------------FQGIYSDQKICKDCPHRYEREEAFMALNL 1847
Cdd:cd02663    62 NYMHQDAHEFLNFLLNEIAEILdaeRKAEKANRKLNNnnnaepqptwvheiFQGILTNETRCLTCETVSSRDETFLDLSI 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1848 GVTSCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWML 1927
Cdd:cd02663   142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1928 NMEpytvagmarqdSSSEVGENGRNMdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDrrgcgKGKWYKF 2006
Cdd:cd02663   222 RLF-----------NTTDDAENPDRL-----------------YELVAVVVHIGGgPNHGHYVSIVKS-----HGGWLLF 268

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568929280 2007 NDTVIEEFDlnDETLEYecFggeyrpkVYDQTNPYTdvrrrywnAYMLFYQ 2057
Cdd:cd02663   269 DDETVEKID--ENAVEE--F-------FGDSPNQAT--------AYVLFYQ 300
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2057 1.86e-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: 1.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVfqqlymqpglpesllsvdddtdnpddsvfyqVQSLFGHlmesklqyyvpenfwkifkmwnkelyvr 1786
Cdd:cd02674     1 GLRNLGNTCYMNSI-------------------------------LQCLSAD---------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1787 eQQDAYEFFTSLIDQMDeylkkmgreQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNL------GVTSCQSLEISLD 1860
Cdd:cd02674    22 -QQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLpipsgsGDAPKVTLEDCLR 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1861 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPW-MLNMEPYtvagmar 1939
Cdd:cd02674    92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLnDLDLTPY------- 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1940 qdsssevgengrnMDQGGGGSPRKkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDE 2019
Cdd:cd02674   163 -------------VDTRSFTGPFK-------YDLYAVVNHYGSLNGGHYTAYCKNNE---TNDWYKFDDSRVTKVSESSV 219

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 568929280 2020 tleyecfggeyrpkvydQTNpytdvrrrywNAYMLFYQ 2057
Cdd:cd02674   220 -----------------VSS----------SAYILFYE 230
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2018 2.65e-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: 2.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENfwKIFK-MWNKELYV 1785
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD--YFLEaSRPPWFTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1786 REQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLeisLDQFVRG 1865
Cdd:cd02664    79 GSQQDCSEYLRYLLDRLHTLIEKM---------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL---LNYFLSP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1866 EVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIK------YDEQIRFPwmlnmepytvagMAR 1939
Cdd:cd02664   147 EKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKimdnvsINEVLSLP------------VRV 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1940 QDSSSEVGENGRNMDQGGGGSprkKVALTENYELVGVIVHSG-QAHAGHYYSF---IKDRRGCGK--------------G 2001
Cdd:cd02664   215 ESKSSESPLEKKEEESGDDGE---LVTRQVHYRLYAVVVHSGySSESGHYFTYardQTDADSTGQecpepkdaeendesK 291

                         330
                  ....*....|....*..
gi 568929280 2002 KWYKFNDTVIEEFDLND 2018
Cdd:cd02664   292 NWYLFNDSRVTFSSFES 308
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2057 2.88e-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: 119.80  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDtdnpddsvfyqvqsLFGHLMESKLQYyvpenfwKIFKmwnkelyvr 1786
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAPQF-------KGYQ--------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1787 eQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEIS----LDQF 1862
Cdd:cd02667    51 -QQDSHELLRYLLDGLRTFIDSI---------FGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECSiescLKQF 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1863 VRGEVLEGSNAYYCEKCKEKRitvKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYtvagMARQDS 1942
Cdd:cd02667   121 TEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPF----CDPKCN 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1943 SSEVGENGRnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDR------------------RGCGKGKWY 2004
Cdd:cd02667   193 SSEDKSSVL-------------------YRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeAGPGSGQWY 253

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568929280 2005 KFNDTVIEEFDLnDETLEYEcfggeyrpkvydqtnpytdvrrrywnAYMLFYQ 2057
Cdd:cd02667   254 YISDSDVREVSL-EEVLKSE--------------------------AYLLFYE 279
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2009 1.07e-25

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 110.11  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYmqpGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLmeSKL-------QYYVPENFW------ 1773
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLF---SIPSFQWRYDDLENKFPSDVVDPANDLNCQL--IKLadgllsgRYSKPASLKsendpy 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1774 ------KIFKM----WNKELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIysDQKI-CKDCPHRY--EREE 1840
Cdd:cd02658    76 qvgikpSMFKAligkGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMI--EDRLeCLSCKKVKytSELS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1841 AFMALNL------------GVTSCQSLEISLDQFVRGEVLEgsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGF- 1907
Cdd:cd02658   154 EILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLl 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1908 -DWesgRSIKYDEQIRFPWMLnmepytvagmarqdsssevgengrnmdqGGGgsprkkvalteNYELVGVIVHSG-QAHA 1985
Cdd:cd02658   230 eNW---VPKKLDVPIDVPEEL----------------------------GPG-----------KYELIAFISHKGtSVHS 267

                         330       340
                  ....*....|....*....|....
gi 568929280 1986 GHYYSFIKdRRGCGKGKWYKFNDT 2009
Cdd:cd02658   268 GHYVAHIK-KEIDGEGKWVLFNDE 290
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2008 8.01e-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: 8.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQV---QSLFGHlMESKLQYYVPENFWKIF------- 1776
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTnalRDLFDT-MDKKQEPVPPIEFLQLLrmafpqf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1777 -KMWNKELYvrEQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKI-CKDCPHRYE---REEAFMALNLGVTS 1851
Cdd:cd02657    80 aEKQNQGGY--AQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMkCTESPDEEEvstESEYKLQCHISITT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1852 -CQSLEISLDQFVRGEVLEGSnayycEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNME 1930
Cdd:cd02657   158 eVNYLQDGLKKGLEEEIEKHS-----PTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568929280 1931 PYtvagmarqdsssevgengrnmdqggggsprkkVALTENYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFND 2008
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 1.50e-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: 1.50e-17
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568929280    6 EQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLT 42
Cdd:cd14286     1 EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT 37
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2057 2.96e-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: 2.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvR 1786
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------L 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1787 EQQDAYEFFTSLIDQMdeylkkmgrEQIFKNTFQGIYSDQKICKDCPHRYE-REEAFMALNLGV-----TSCQSLEISLD 1860
Cdd:cd02662    33 EQQDAHELFQVLLETL---------EQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVpnqssGSGTTLEHCLD 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1861 QFVRGEVLEGsnaYYCEKCKEKritvkrtcIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLnmepytvagmarq 1940
Cdd:cd02662   104 DFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERL------------- 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1941 dsssevgengrnmdqggggsPRKKvaltenYELVGVIVHSGQAHAGHYYSF-----------------IKDRRGCGKGKW 2003
Cdd:cd02662   159 --------------------PKVL------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrMREGPSSTSHPW 212

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568929280 2004 YKFNDTVIEEFDLNDETLEYEcfggeyrpkvydqtnpytdvrrrywnAYMLFYQ 2057
Cdd:cd02662   213 WRISDTTVKEVSESEVLEQKS--------------------------AYMLFYE 240
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1680-2015 7.95e-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: 84.56  E-value: 7.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1680 HHQPDPALTkefdyLPPVDSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDdsvfyQVQSLFGHL 1759
Cdd:cd02671     4 VPAPQPSSA-----TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVE-----QLQSSFLLN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1760 ME---SKLQYYVPENFWKIFKMWNKELYVREQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKICKDCPHRY 1836
Cdd:cd02671    74 PEkynDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKD---------FQGQLVLRTRCLECETFT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1837 EREEAFMALNLGV------TSCQSLEISLD-------------QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSV 1897
Cdd:cd02671   145 ERREDFQDISVPVqeselsKSEESSEISPDpktemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1898 LVIHLMRFG-----FDWESGRSiKYDEQIRFPWMLNMEpytvagmarqdsssevgengrnmdqGGGGSPRKKValtenYE 1972
Cdd:cd02671   225 ITIHLKCFAangseFDCYGGLS-KVNTPLLTPLKLSLE-------------------------EWSTKPKNDV-----YR 273

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568929280 1973 LVGVIVHSG-QAHAGHYYSFIkdrrgcgkgKWYKFNDT---VIEEFD 2015
Cdd:cd02671   274 LFAVVMHSGaTISSGHYTAYV---------RWLLFDDSevkVTEEKD 311
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1706-2011 1.20e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 74.23  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1706 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENFWKIFKMW--NKEL 1783
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeASAL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1784 ----YVREQQDAyEFFTSLI--------DQM-DEYLKKMGREQ----IFKNTFQGIYSDQKICKDCPHRYEREEAFMALN 1846
Cdd:pfam13423   81 glldEDRETNSA-ISLSSLIqsfnrfllDQLsSEENSTPPNPSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1847 L--------------GVTSCQSLEISLDQfvrgevlEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESG 1912
Cdd:pfam13423  160 LiyprkpssnnkkppNQTFSSILKSSLER-------ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280  1913 RSIKydeqirfPWmLNMEPYTVagmarqdsssevgengrnMDQGGGGSPRKKValtenYELVGVIVH-SGQAHAGHYYSF 1991
Cdd:pfam13423  233 WKTP-------GW-LPPEIGLT------------------LSDDLQGDNEIVK-----YELRGVVVHiGDSGTSGHLVSF 281

                          330       340
                   ....*....|....*....|....
gi 568929280  1992 IK----DRRGCGKGKWYKFNDTVI 2011
Cdd:pfam13423  282 VKvadsELEDPTESQWYLFNDFLV 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1854-2060 4.22e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 75.30  E-value: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1854 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRfgFDWESGRSIKYDEQIRFPWM-LNMEPY 1932
Cdd:COG5560   676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIDdLDLSGV 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1933 TVAGMarqdsSSEVGengrnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgCGKGKWYKFNDTVIE 2012
Cdd:COG5560   754 EYMVD-----DPRLI-----------------------YDLYAVDNHYGGLSGGHYTAYARN---FANNGWYLFDDSRIT 802

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568929280 2013 EFDLNDETLEyecfggeyrpkvydqtnpytdvrrrywNAYMLFYQRVS 2060
Cdd:COG5560   803 EVDPEDSVTS---------------------------SAYVLFYRRKS 823
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1707-2008 2.52e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 67.13  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQL-YMQPGLPESLLsvdddTDNPDDSVFYQV-----QSLFGHLMESKLQYYVPENFWKIFKMWN 1780
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILaLYLPKLDELLD-----DLSKELKVLKNVirkpePDLNQEEALKLFTALWSSKEHKVGWIPP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1781 KElyvrEQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTfqgiysdqkicKDCPHRYEREeaFMALNLGVTSCQSLEIS-- 1858
Cdd:COG5533    76 MG----SQEDAHELLGKLLDELKLDLVNSFTIRIFKTT-----------KDKKKTSTGD--WFDIIIELPDQTWVNNLkt 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1859 LDQFvrgevLEGSNAYYCEKC-------KEKRITVKR---TCIKSLPSVLVIHLMRFGFDwesGRSIKYDEQIRfpwmln 1928
Cdd:COG5533   139 LQEF-----IDNMEELVDDETgvkakenEELEVQAKQeyeVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1929 mEPYTVAgmARQDSSSEVGENGRnmdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgcgKGKWYKFND 2008
Cdd:COG5533   205 -EKFELP--VKHDQILNIVKETY-------------------YDLVGFVLHQGSLEGGHYIAYVKK-----GGKWEKAND 257
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1707-2035 2.59e-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: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1707 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklQYYVPENFWKIFKmWnkelyvr 1786
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSLFSQ-------------------------------------QQDVSEFTHLLLD-W------- 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1787 eQQDAYEFFTSLIDQMDEYLKKMgrEQIFKNTF--QGIYSDQKICKDcphryereEAFMALNLGVTSCQSLEISLD-QFV 1863
Cdd:cd02665    36 -LEDAFQAAAEAISPGEKSKNPM--VQLFYGTFltEGVLEGKPFCNC--------ETFGQYPLQVNGYGNLHECLEaAMF 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1864 RGEVlEGSNAYYCEKCKEKRITVKrtciksLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPWMLNMEPYtvagmarqdss 1943
Cdd:cd02665   105 EGEV-ELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQVPY----------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1944 sevgengrnmdqggggsprkkvaltenyELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLndETLEY 2023
Cdd:cd02665   165 ----------------------------ELHAVLVHEGQANAGHYWAYIYKQS---RQEWEKYNDISVTESSW--EEVER 211

                         330
                  ....*....|..
gi 568929280 2024 ECFGGEYRPKVY 2035
Cdd:cd02665   212 DSFGGGRNPSAY 223
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 979-1049 1.03e-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: 51.06  E-value: 1.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568929280  979 LNVTYESTKdTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLtvnKDQKLLHQLGFSDEQVLTV 1049
Cdd:cd17039     1 ITVKTLDGK-TYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKEL---KDDKTLSDYGIKDGSTIHL 67
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1787-2057 1.18e-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: 55.23  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1787 EQQDAYEFFTSLIDQMDEYLKKMgreqifkntFQGIYSDQKickdcphRYEREEAFMalnlgvtSCQSLEISLDQFVRGE 1866
Cdd:cd02670    22 EQQDPEEFFNFITDKLLMPLLEP---------KVDIIHGGK-------KDQDDDKLV-------NERLLQIPVPDDDDGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1867 VLEgsnayyCEKCKEKRITVKRtcIKSLPSVLVIHLMRFGfdWESGRSIKYDEQIRFPWMLNMePYTVAGMARQDS--SS 1944
Cdd:cd02670    79 GIT------LEQCLEQYFNNSV--FAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDI-PDFVADDPRACSkcQL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1945 EVGENGRNMDQGGGGSPRKKValtenyeLVGVIVHSGQA-HAGHYYSFIK--------DRRGCGKGKWYKFNDtvieefd 2015
Cdd:cd02670   148 ECRVCYDDKDFSPTCGKFKLS-------LCSAVCHRGTSlETGHYVAFVRygsyslteTDNEAYNAQWVFFDD------- 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568929280 2016 LNDetleyecfggeyRPKVYDQTNpyTDVRRRYWNAYMLFYQ 2057
Cdd:cd02670   214 MAD------------RDGVSNGFN--IPAARLLEDPYMLFYQ 241
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1971-2021 3.26e-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: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568929280 1971 YELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVIEEFDLNDETL 2021
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDF---EENVWRKYNDETVTVVPASEVFL 328
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1853-2024 5.32e-04

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 44.43  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1853 QSLEISLDQFVrgevlegSNAYYCEKCKEKRITVKRTCIKSLP----SVLVIHLMRFGfdweSGRSIKYDEQIRFPWMLN 1928
Cdd:cd02672   121 QLLKRSLDLEK-------VTKAWCDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTN----GEFDDINVVLPSGKVMQN 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1929 MEPYtvagmARQDSSSEVGENGRNMdqggggsprkkvalTENYELVGVIVH-SGQAHAGHYYSF-IKDRRGCGKGKWYKF 2006
Cdd:cd02672   190 KVSP-----KAIDHDKLVKNRGQES--------------IYKYELVGYVCEiNDSSRGQHNVVFvIKVNEESTHGRWYLF 250

                         170
                  ....*....|....*...
gi 568929280 2007 NDTVIEEFDLNDETLEYE 2024
Cdd:cd02672   251 NDFLVTPVSELAYILLYQ 268
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1704-1809 3.10e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 42.95  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1704 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS---VDDDTDNPDDSVFYQVQSLFGHLMES----KLQYYVPENFWKIF 1776
Cdd:COG5560   264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdeyEESINEENPLGMHGSVASAYADLIKQlydgNLHAFTPSGFKKTI 343

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568929280 1777 KMWNKELYVREQQDAYEFFTSLIDQMDEYLKKM 1809
Cdd:COG5560   344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRI 376
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 11-41 3.99e-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: 3.99e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568929280   11 TLLCMGFSdPATIRKALRLAKNDINEAVALL 41
Cdd:cd14297     6 QLVDMGFT-EAQARKALRKTNNNVERAVDWL 35
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 1666-2013 4.69e-03

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 41.92  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1666 PSNLQIITKELLSMHHQPDPALTKE----FDYLPPV-----DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS 1736
Cdd:cd02669    71 PDNYEIIDSSLDDIKYVLNPTYTKEqisdLDRDPKLsrdldGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1737 V-DDDTDNPDDSVFYQVQS-LFGHLMESKL--QYYVPENFWKIFKMW-NKELYVREQQDAYEFFTSLIDQMDEYLKKMGR 1811
Cdd:cd02669   151 YeNYENIKDRKSELVKRLSeLIRKIWNPRNfkGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKK 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1812 --EQIFKNTFQG---IYSdQKIckdcPHRYEREEAFMALNLGVTSCQS-----LEISLD-----------------QFVR 1864
Cdd:cd02669   231 pnSSIIHDCFQGkvqIET-QKI----KPHAEEEGSKDKFFKDSRVKKTsvspfLLLTLDlpppplfkdgneeniipQVPL 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568929280 1865 GEVLEGsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFgfdwESGRSIKYDEQ--IRFPWMLNMEPYTVAGMARQDS 1942
Cdd:cd02669   306 KQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRF----SKNNFFKEKNPtiVNFPIKNLDLSDYVHFDKPSLN 378

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568929280 1943 SSevgengrnmdqggggsprkkvaltENYELVGVIVHSGQAH-AGHYYSFIKDRrgcGKGKWYKFNDTVIEE 2013
Cdd:cd02669   379 LS------------------------TKYNLVANIVHEGTPQeDGTWRVQLRHK---STNKWFEIQDLNVKE 423
 
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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