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Conserved domains on  [gi|2217265894|ref|XP_047272480|]
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ubiquitin carboxyl-terminal hydrolase 24 isoform X3 [Homo sapiens]

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 ...
1686-2043 5.35e-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: 466.35  E-value: 5.35e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1686 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1762
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1763 KELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1842
Cdd:cd02659     79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1843 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVSGMARQ 1922
Cdd:cd02659    159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1923 DsssevgengrsvdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2002
Cdd:cd02659    239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2217265894 2003 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2043
Cdd:cd02659    297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
954-1032 1.72e-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: 153.23  E-value: 1.72e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265894  954 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQILTVK 1032
Cdd:cd17065      1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
6-42 1.49e-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: 1.49e-17
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217265894    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 ...
1686-2043 5.35e-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: 466.35  E-value: 5.35e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1686 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1762
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1763 KELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1842
Cdd:cd02659     79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1843 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVSGMARQ 1922
Cdd:cd02659    159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1923 DsssevgengrsvdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2002
Cdd:cd02659    239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2217265894 2003 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2043
Cdd:cd02659    297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1688-2038 2.23e-66

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 228.10  E-value: 2.23e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1688 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1762
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1763 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---RDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1833
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1834 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1913
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1914 YTVSGMArqdsssevgengrsvdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 1993
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2217265894 1994 EEFDLNDETLEyecfggeyrpkvydqtnpytdvrrryWNAYMLFY 2038
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
954-1032 1.72e-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: 153.23  E-value: 1.72e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265894  954 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQILTVK 1032
Cdd:cd17065      1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1680-2140 1.43e-39

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 161.96  E-value: 1.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1680 DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1759
Cdd:COG5077    186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1760 MWNKELYVReQQDAYEFFTSLIDQMDeylKKMgRDQIFKNTFQGI---YSDQKI-CKDCPHRYEREEAFMALNLGVTSCQ 1835
Cdd:COG5077    264 GWDSDDSFM-QHDIQEFNRVLQDNLE---KSM-RGTVVENALNGIfvgKMKSYIkCVNVNYESARVEDFWDIQLNVKGMK 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1836 SLEISLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEP 1913
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLP 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1914 YTvsgmarqDSSSEVGENGRSVdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVI 1993
Cdd:COG5077    416 FL-------DRDADKSENSDAV-----------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRV 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1994 EEFDLNdETLEyECFGGE--YRPKVYDQTNPytdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPS 2071
Cdd:COG5077    469 TRATEK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVA 522
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265894 2072 SPEISPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2140
Cdd:COG5077    523 AVDIPPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
6-42 1.49e-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: 1.49e-17
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217265894    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 ...
1686-2043 5.35e-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: 466.35  E-value: 5.35e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1686 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1762
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1763 KELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1842
Cdd:cd02659     79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1843 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVSGMARQ 1922
Cdd:cd02659    159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1923 DsssevgengrsvdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2002
Cdd:cd02659    239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2217265894 2003 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2043
Cdd:cd02659    297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1688-2038 2.23e-66

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 228.10  E-value: 2.23e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1688 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1762
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1763 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---RDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1833
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1834 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1913
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1914 YTVSGMArqdsssevgengrsvdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 1993
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2217265894 1994 EEFDLNDETLEyecfggeyrpkvydqtnpytdvrrryWNAYMLFY 2038
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1689-2039 1.58e-59

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


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 206.18  E-value: 1.58e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvr 1768
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1769 eQQDAYEFFTSLIDQMDEYLKKMGR--------DQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGV----TSCQS 1836
Cdd:cd02257     22 -QQDAHEFLLFLLDKLHEELKKSSKrtsdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVS 100
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1837 LEISLDQFVRGEVLEGSNAYYCEKCKeKRITVKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTV 1916
Cdd:cd02257    101 LEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLS 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1917 SGMARQDSSSEVGengrsvdqggggsprkkvalteNYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFNDTVIEE 1995
Cdd:cd02257    179 EGEKDSDSDNGSY----------------------KYELVAVVVHSGTsADSGHYVAYVKDP---SDGKWYKFNDDKVTE 233
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2217265894 1996 FDLNDEtleyecfggeyrpkvydqtnpyTDVRRRYWNAYMLFYQ 2039
Cdd:cd02257    234 VSEEEV----------------------LEFGSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2038 8.17e-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: 178.00  E-value: 8.17e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS-----------VFYQVQSLFGHLMESKLQYYVPENFWKI 1757
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepqtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1758 FkmwnkELYVREQQDAYEF---FTSLIDqmDEYLKKMGRD--QIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVT 1832
Cdd:cd02668     81 L-----GLDTGQQQDAQEFsklFLSLLE--AKLSKSKNPDlkNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1833 SCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNME 1912
Cdd:cd02668    154 GHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1913 PYtvsgMARQDSSSEVgengrsvdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRRgcgKGKWYKFNDT 1991
Cdd:cd02668    234 EY----LAESDEGSYV------------------------YELSGVLIHQGVsAYSGHYIAHIKDEQ---TGEWYKFNDE 282
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217265894 1992 VIEE-----FDLNDETLEYECFGGEYRPKVYDQTnpytdvrrrywNAYMLFY 2038
Cdd:cd02668    283 DVEEmpgkpLKLGNSEDPAKPRKSEIKKGTHSSR-----------TAYMLVY 323
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2038 1.06e-43

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 162.45  E-value: 1.06e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS--VFYQVQSLFGHLMESKLQYYVPENFWKIFKMWNKELY 1766
Cdd:cd02661      3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1767 VREQQDAYEFFTSLIDQM-----DEYLKKMGRDQIFKNT------FQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ 1835
Cdd:cd02661     83 IGRQEDAHEFLRYLLDAMqkaclDRFKKLKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1836 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFdwesGRSIKYDEQIRFPWMLNMEPYt 1915
Cdd:cd02661    163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQISFPETLDLSPY- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1916 vsgmarqdsssevgengrsVDQGGGGSPRkkvaltenYELVGVIVHSG-QAHAGHYYSFIKDRRgcgkGKWYKFNDTVIE 1994
Cdd:cd02661    238 -------------------MSQPNDGPLK--------YKLYAVLVHSGfSPHSGHYYCYVKSSN----GKWYNMDDSKVS 286
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2217265894 1995 EFDLNDetleyecfggeyrpkVYDQtnpytdvrrrywNAYMLFY 2038
Cdd:cd02661    287 PVSIET---------------VLSQ------------KAYILFY 303
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
954-1032 1.72e-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: 153.23  E-value: 1.72e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265894  954 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQILTVK 1032
Cdd:cd17065      1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2038 6.68e-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: 155.22  E-value: 6.68e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV--------------FYQVQSLFGHLMESKLQyyvpeNF 1754
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsclscamdeifqeFYYSGDRSPYGPINLLY-----LS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1755 WKIfkmwNKELYVREQQDAYEFFTSLIDQM--------DEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMA 1826
Cdd:cd02660     77 WKH----SRNLAGYSQQDAHEFFQFLLDQLhthyggdkNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1827 LNL---------------GVTSCQSLEISLDQFVRGEVLeGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDw 1891
Cdd:cd02660    153 LSLdipnkstpswalgesGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS- 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1892 ESGRSIKYDEQIRFPWMLNMEPYTVSGMARQDSSSEVgengrsvdqggggSPRKKvaltenYELVGVIVHSGQAHAGHYY 1971
Cdd:cd02660    231 LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSL-------------DPDYT------YDLFAVVVHKGTLDTGHYT 291
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217265894 1972 SFIKDrrgcGKGKWYKFNDTVIEEFDLNDetleyecfggeyrpkVYDQtnpytdvrrrywNAYMLFY 2038
Cdd:cd02660    292 AYCRQ----GDGQWFKFDDAMITRVSEEE---------------VLKS------------QAYLLFY 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1680-2140 1.43e-39

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 161.96  E-value: 1.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1680 DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1759
Cdd:COG5077    186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1760 MWNKELYVReQQDAYEFFTSLIDQMDeylKKMgRDQIFKNTFQGI---YSDQKI-CKDCPHRYEREEAFMALNLGVTSCQ 1835
Cdd:COG5077    264 GWDSDDSFM-QHDIQEFNRVLQDNLE---KSM-RGTVVENALNGIfvgKMKSYIkCVNVNYESARVEDFWDIQLNVKGMK 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1836 SLEISLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEP 1913
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLP 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1914 YTvsgmarqDSSSEVGENGRSVdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVI 1993
Cdd:COG5077    416 FL-------DRDADKSENSDAV-----------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRV 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1994 EEFDLNdETLEyECFGGE--YRPKVYDQTNPytdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPS 2071
Cdd:COG5077    469 TRATEK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVA 522
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265894 2072 SPEISPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2140
Cdd:COG5077    523 AVDIPPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2039 7.86e-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: 145.15  E-value: 7.86e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYmqpglpesllsvdddtdnpDDSVFYQVQSLFGHLMESKLQYYV--PENFWKIFKMWNKELY 1766
Cdd:cd02663      1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENELFD 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1767 VREQQDAYEFFTSLIDQMDEYLKK------MGRDQIFKNT-----------FQGIYSDQKICKDCPHRYEREEAFMALNL 1829
Cdd:cd02663     62 NYMHQDAHEFLNFLLNEIAEILDAerkaekANRKLNNNNNaepqptwvheiFQGILTNETRCLTCETVSSRDETFLDLSI 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1830 GVTSCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWML 1909
Cdd:cd02663    142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1910 NMEpytvsgmarqdSSSEVGENgrsvdqggggsprkkvaLTENYELVGVIVHSGQ-AHAGHYYSFIKDrrgcgKGKWYKF 1988
Cdd:cd02663    222 RLF-----------NTTDDAEN-----------------PDRLYELVAVVVHIGGgPNHGHYVSIVKS-----HGGWLLF 268
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217265894 1989 NDTVIEEFDlnDETLEYecFggeyrpkVYDQTNPYTdvrrrywnAYMLFYQ 2039
Cdd:cd02663    269 DDETVEKID--ENAVEE--F-------FGDSPNQAT--------AYVLFYQ 300
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2039 1.10e-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: 139.73  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVfqqlymqpglpesllsvdddtdnpddsvfyqVQSLFGHlmesklqyyvpenfwkifkmwnkelyvr 1768
Cdd:cd02674      1 GLRNLGNTCYMNSI-------------------------------LQCLSAD---------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1769 eQQDAYEFFTSLIDQMDeylkkmgrdQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNL------GVTSCQSLEISLD 1842
Cdd:cd02674     22 -QQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLpipsgsGDAPKVTLEDCLR 91
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1843 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPW-MLNMEPYtvsgmar 1921
Cdd:cd02674     92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLnDLDLTPY------- 162
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1922 qdsssevgengrsVDQGGGGSPRKkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDE 2001
Cdd:cd02674    163 -------------VDTRSFTGPFK-------YDLYAVVNHYGSLNGGHYTAYCKNNE---TNDWYKFDDSRVTKVSESSV 219
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2217265894 2002 tleyecfggeyrpkvydQTNpytdvrrrywNAYMLFYQ 2039
Cdd:cd02674    220 -----------------VSS----------SAYILFYE 230
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2000 9.67e-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: 137.24  E-value: 9.67e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENfwKIFK-MWNKELYV 1767
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD--YFLEaSRPPWFTP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1768 REQQDAYEFFTSLIDQMDEYLKKMgrdqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLeisLDQFVRG 1847
Cdd:cd02664     79 GSQQDCSEYLRYLLDRLHTLIEKM---------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL---LNYFLSP 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1848 EVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMepyTVSGMARQDSSSE 1927
Cdd:cd02664    147 EKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSL---PVRVESKSSESPL 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1928 VGENGRSVDQGGGgsprkkVALTENYELVGVIVHSG-QAHAGHYYSF---IKDRRGCGK--------------GKWYKFN 1989
Cdd:cd02664    224 EKKEEESGDDGEL------VTRQVHYRLYAVVVHSGySSESGHYFTYardQTDADSTGQecpepkdaeendesKNWYLFN 297
                          330
                   ....*....|.
gi 2217265894 1990 DTVIEEFDLND 2000
Cdd:cd02664    298 DSRVTFSSFES 308
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2039 2.19e-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: 120.18  E-value: 2.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDtdnpddsvfyqvqsLFGHLMESKLQYyvpenfwKIFKmwnkelyvr 1768
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAPQF-------KGYQ--------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1769 eQQDAYEFFTSLIDQMDEYLkkmgrDQIFKntfqGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ----SLEISLDQF 1844
Cdd:cd02667     51 -QQDSHELLRYLLDGLRTFI-----DSIFG----GELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIksecSIESCLKQF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1845 VRGEVLEGSNAYYCEKCKEKRitvKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTvsgmarqDS 1924
Cdd:cd02667    121 TEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFC-------DP 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1925 SSEVGENGRSVdqggggsprkkvalteNYELVGVIVHSGQAHAGHYYSFIKDR------------------RGCGKGKWY 1986
Cdd:cd02667    190 KCNSSEDKSSV----------------LYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeAGPGSGQWY 253
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217265894 1987 KFNDTVIEEFDLnDETLEYEcfggeyrpkvydqtnpytdvrrrywnAYMLFYQ 2039
Cdd:cd02667    254 YISDSDVREVSL-EEVLKSE--------------------------AYLLFYE 279
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-1991 6.54e-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: 110.88  E-value: 6.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYmqpGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLmeSKL-------QYYVPENFW------ 1755
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLF---SIPSFQWRYDDLENKFPSDVVDPANDLNCQL--IKLadgllsgRYSKPASLKsendpy 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1756 ------KIFKM----WNKELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIysDQKI-CKDCPHRY--EREE 1822
Cdd:cd02658     76 qvgikpSMFKAligkGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMI--EDRLeCLSCKKVKytSELS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1823 AFMALNL------------GVTSCQSLEISLDQFVRGEVLEgsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGF- 1889
Cdd:cd02658    154 EILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLl 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1890 -DWesgRSIKYDEQIRFPWMLnmepytvsgmarqdsssevgengrsvdqGGGgsprkkvalteNYELVGVIVHSG-QAHA 1967
Cdd:cd02658    230 eNW---VPKKLDVPIDVPEEL----------------------------GPG-----------KYELIAFISHKGtSVHS 267
                          330       340
                   ....*....|....*....|....
gi 2217265894 1968 GHYYSFIKdRRGCGKGKWYKFNDT 1991
Cdd:cd02658    268 GHYVAHIK-KEIDGEGKWVLFNDE 290
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-1990 1.36e-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: 92.01  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQV---QSLFGHlMESKLQYYVPENFWKIF------- 1758
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTnalRDLFDT-MDKKQEPVPPIEFLQLLrmafpqf 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1759 -KMWNKELYvrEQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKI-CKDCPHRYE---REEAFMALNLGVTS 1833
Cdd:cd02657     80 aEKQNQGGY--AQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMkCTESPDEEEvstESEYKLQCHISITT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1834 -CQSLEISLDQFVRGEVLEGSnayycEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNM- 1911
Cdd:cd02657    158 eVNYLQDGLKKGLEEEIEKHS-----PTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLy 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1912 EPYTVSGMarqdsssevgengrsvdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFND 1990
Cdd:cd02657    233 ELCTPSGY---------------------------------YELVAVITHQGRsADSGHYVAWVRRK---NDGKWIKFDD 276
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
6-42 1.49e-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: 1.49e-17
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217265894    6 EQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLT 42
Cdd:cd14286      1 EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT 37
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1662-1997 7.97e-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: 7.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1662 HHQPDPALTkefdyLPPVDSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDdsvfyQVQSLFGHL 1741
Cdd:cd02671      4 VPAPQPSSA-----TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVE-----QLQSSFLLN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1742 ME---SKLQYYVPENFWKIFKMWNKELYVREQQDAYEFFTSLIDQMDEYLKKMgrdqifkntFQGIYSDQKICKDCPHRY 1818
Cdd:cd02671     74 PEkynDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKD---------FQGQLVLRTRCLECETFT 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1819 EREEAFMALNLGV------TSCQSLEISLD-------------QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSV 1879
Cdd:cd02671    145 ERREDFQDISVPVqeselsKSEESSEISPDpktemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1880 LVIHLMRFG-----FDWESGRSiKYDEQIRFPWMLNMEpytvsgmarqdsssevgengrsvdqGGGGSPRKKValtenYE 1954
Cdd:cd02671    225 ITIHLKCFAangseFDCYGGLS-KVNTPLLTPLKLSLE-------------------------EWSTKPKNDV-----YR 273
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2217265894 1955 LVGVIVHSG-QAHAGHYYSFIkdrrgcgkgKWYKFNDT---VIEEFD 1997
Cdd:cd02671    274 LFAVVMHSGaTISSGHYTAYV---------RWLLFDDSevkVTEEKD 311
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2039 8.98e-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: 82.41  E-value: 8.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvR 1768
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------L 32
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1769 EQQDAYEFFTSLIDQMdeylkkmgrDQIFKNTFQGIYSDQKICKDCPHRYE-REEAFMALNLGV-----TSCQSLEISLD 1842
Cdd:cd02662     33 EQQDAHELFQVLLETL---------EQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVpnqssGSGTTLEHCLD 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1843 QFVRGEVLEGsnaYYCEKCKEKritvkrtcIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLnmepytvsgmarq 1922
Cdd:cd02662    104 DFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERL------------- 158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1923 dsssevgengrsvdqggggsPRKKvaltenYELVGVIVHSGQAHAGHYYSF-----------------IKDRRGCGKGKW 1985
Cdd:cd02662    159 --------------------PKVL------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrMREGPSSTSHPW 212
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217265894 1986 YKFNDTVIEEFDLNDETLEYEcfggeyrpkvydqtnpytdvrrrywnAYMLFYQ 2039
Cdd:cd02662    213 WRISDTTVKEVSESEVLEQKS--------------------------AYMLFYE 240
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1688-1993 1.03e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 74.61  E-value: 1.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1688 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENFWKIFKMW--NKEL 1765
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1766 ----YVREQQDAyEFFTSLI--------DQM-DEYLKKMGRDQ----IFKNTFQGIYSDQKICKDCPHRYEREEAFMALN 1828
Cdd:pfam13423   81 glldEDRETNSA-ISLSSLIqsfnrfllDQLsSEENSTPPNPSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1829 L--------------GVTSCQSLEISLDQfvrgevlEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESG 1894
Cdd:pfam13423  160 LiyprkpssnnkkppNQTFSSILKSSLER-------ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1895 RSIKydeqirfPWmLNMEPYTvsgmarqdsssevgengrSVDQGGGGSPRKKValtenYELVGVIVH-SGQAHAGHYYSF 1973
Cdd:pfam13423  233 WKTP-------GW-LPPEIGL------------------TLSDDLQGDNEIVK-----YELRGVVVHiGDSGTSGHLVSF 281
                          330       340
                   ....*....|....*....|....
gi 2217265894 1974 IK----DRRGCGKGKWYKFNDTVI 1993
Cdd:pfam13423  282 VKvadsELEDPTESQWYLFNDFLV 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1836-2042 2.20e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 76.08  E-value: 2.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1836 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRfgFDWESGRSIKYDEQIRFPWM-LNMEPY 1914
Cdd:COG5560    676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIDdLDLSGV 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1915 TVSGMarqdsSSEVGengrsvdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgCGKGKWYKFNDTVIE 1994
Cdd:COG5560    754 EYMVD-----DPRLI-----------------------YDLYAVDNHYGGLSGGHYTAYARN---FANNGWYLFDDSRIT 802
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2217265894 1995 EFDLNDETLEyecfggeyrpkvydqtnpytdvrrrywNAYMLFYQRVS 2042
Cdd:COG5560    803 EVDPEDSVTS---------------------------SAYVLFYRRKS 823
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1689-1990 8.07e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 68.68  E-value: 8.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQL-YMQPGLPESLLsvdddTDNPDDSVFYQV-----QSLFGHLMESKLQYYVPENFWKIFKMWN 1762
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILaLYLPKLDELLD-----DLSKELKVLKNVirkpePDLNQEEALKLFTALWSSKEHKVGWIPP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1763 KElyvrEQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTfqgiysdqkicKDCPHRYEREeaFMALNLGVTSCQSLEIS-- 1840
Cdd:COG5533     76 MG----SQEDAHELLGKLLDELKLDLVNSFTIRIFKTT-----------KDKKKTSTGD--WFDIIIELPDQTWVNNLkt 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1841 LDQFvrgevLEGSNAYYCEKC-------KEKRITVKR---TCIKSLPSVLVIHLMRFGFDwesGRSIKYDEQIRfpwmln 1910
Cdd:COG5533    139 LQEF-----IDNMEELVDDETgvkakenEELEVQAKQeyeVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD------ 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1911 mEPYTVSgmARQDSSSEVGENGRsvdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgcgKGKWYKFND 1990
Cdd:COG5533    205 -EKFELP--VKHDQILNIVKETY-------------------YDLVGFVLHQGSLEGGHYIAYVKK-----GGKWEKAND 257
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1689-2017 2.43e-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: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1689 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklQYYVPENFWKIFKmWnkelyvr 1768
Cdd:cd02665      1 GLKNVGNTCWFSAVIQSLFSQ-------------------------------------QQDVSEFTHLLLD-W------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1769 eQQDAYEFFTSLIDQMDEYLKKMGrdQIFKNTF--QGIYSDQKICKDcphryereEAFMALNLGVTSCQSLEISLD-QFV 1845
Cdd:cd02665     36 -LEDAFQAAAEAISPGEKSKNPMV--QLFYGTFltEGVLEGKPFCNC--------ETFGQYPLQVNGYGNLHECLEaAMF 104
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1846 RGEVlEGSNAYYCEKCKEKRITVKrtciksLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPWMLNMEPYtvsgmarqdss 1925
Cdd:cd02665    105 EGEV-ELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQVPY----------- 164
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1926 sevgengrsvdqggggsprkkvaltenyELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLndETLEY 2005
Cdd:cd02665    165 ----------------------------ELHAVLVHEGQANAGHYWAYIYKQS---RQEWEKYNDISVTESSW--EEVER 211
                          330
                   ....*....|..
gi 2217265894 2006 ECFGGEYRPKVY 2017
Cdd:cd02665    212 DSFGGGRNPSAY 223
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
961-1031 1.32e-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: 1.32e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217265894  961 LNVTYESTKdTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLtvnKDQKLLHQLGFSDEQILTV 1031
Cdd:cd17039      1 ITVKTLDGK-TYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKEL---KDDKTLSDYGIKDGSTIHL 67
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1688-2003 5.88e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 54.03  E-value: 5.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1688 VGLRNGGATCYMNAVFQQLYMQPGLPESLLS----------------------VDDDTDNPDDSVFYQVQSLFGHLMESK 1745
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeskaelasdypterriggreVSRSELQRSNQFVYELRSLFNDLIHSN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1746 LQYYVPEnfwkifkmwnKEL--YVREQQDAYEFFTSLIDQMDEYLK-----KMGRDQI--------FKNTFQGIYsDQKI 1810
Cdd:cd02666     82 TRSVTPS----------KELayLALRQQDVTECIDNVLFQLEVALEpisnaFAGPDTEddkeqsdlIKRLFSGKT-KQQL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1811 CKD----CPHRYEREEAFMALNLGVTSC----------QSLEISLDQFVRGEVLEgsnayycekckekritvkrtcikSL 1876
Cdd:cd02666    151 VPEsmgnQPSVRTKTERFLSLLVDVGKKgreivvllepKDLYDALDRYFDYDSLT-----------------------KL 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1877 PSVLVIHLMRFGFdwesgrsiKYDEQIrfpWMLNMEPYTVSgmarQDSSSEVGENGRSVDQGGGGSPRKKVALTEN---- 1952
Cdd:cd02666    208 PQRSQVQAQLAQP--------LQRELI---SMDRYELPSSI----DDIDELIREAIQSESSLVRQAQNELAELKHEiekq 272
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265894 1953 --------YELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVIEEFDLNDETL 2003
Cdd:cd02666    273 fddlksygYRLHAVFIHRGEASSGHYWVYIKDF---EENVWRKYNDETVTVVPASEVFL 328
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1769-2039 3.25e-06

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 50.99  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1769 EQQDAYEFFTSLIDQMDEYLKKMGRDqifkntfqgIYSDQKickdcphRYEREEAFMalnlgvtSCQSLEISLDQFVRGE 1848
Cdd:cd02670     22 EQQDPEEFFNFITDKLLMPLLEPKVD---------IIHGGK-------KDQDDDKLV-------NERLLQIPVPDDDDGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1849 VLEgsnayyCEKCKEKRITVKRtcIKSLPSVLVIHLMRFGfdWESGRSIKYDEQIRFPWMLNMePYTVSGMARQDS--SS 1926
Cdd:cd02670     79 GIT------LEQCLEQYFNNSV--FAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDI-PDFVADDPRACSkcQL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1927 EVGENGRSVDQGGGGSPRKKValtenyeLVGVIVHSGQA-HAGHYYSFIK--------DRRGCGKGKWYKFNDtvieefd 1997
Cdd:cd02670    148 ECRVCYDDKDFSPTCGKFKLS-------LCSAVCHRGTSlETGHYVAFVRygsyslteTDNEAYNAQWVFFDD------- 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2217265894 1998 LNDetleyecfggeyRPKVYDQTNpyTDVRRRYWNAYMLFYQ 2039
Cdd:cd02670    214 MAD------------RDGVSNGFN--IPAARLLEDPYMLFYQ 241
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1835-2006 4.71e-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: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1835 QSLEISLDQFVrgevlegSNAYYCEKCKEKRITVKRTCIKSLP----SVLVIHLMRFGFDWESGRSIkydeqirfpwmln 1910
Cdd:cd02672    121 QLLKRSLDLEK-------VTKAWCDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVV------------- 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1911 mEPYTVSGMARqDSSSEvGENGRSVDQGGGGSPRKkvaltenYELVGVIVH-SGQAHAGHYYSF-IKDRRGCGKGKWYKF 1988
Cdd:cd02672    181 -LPSGKVMQNK-VSPKA-IDHDKLVKNRGQESIYK-------YELVGYVCEiNDSSRGQHNVVFvIKVNEESTHGRWYLF 250
                          170
                   ....*....|....*...
gi 2217265894 1989 NDTVIEEFDLNDETLEYE 2006
Cdd:cd02672    251 NDFLVTPVSELAYILLYQ 268
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1686-1829 2.64e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.33  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1686 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS---VDDDTDNPDDSVFYQVQSLFGHLMES----KLQYYVPENFWKIF 1758
Cdd:COG5560    264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdeyEESINEENPLGMHGSVASAYADLIKQlydgNLHAFTPSGFKKTI 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1759 KMWNKELYVREQQDAYEFFTSLIDQMDEYLKKM-------------GRDQIFKNT-------------------FQGIYS 1806
Cdd:COG5560    344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIikkpytskpdlspGDDVVVKKKakecwwehlkrndsiitdlFQGMYK 423
                          170       180
                   ....*....|....*....|...
gi 2217265894 1807 DQKICKDCPHRYEREEAFMALNL 1829
Cdd:COG5560    424 STLTCPGCGSVSITFDPFMDLTL 446
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
11-41 3.85e-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: 3.85e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217265894   11 TLLCMGFSdPATIRKALRLAKNDINEAVALL 41
Cdd:cd14297      6 QLVDMGFT-EAQARKALRKTNNNVERAVDWL 35
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1648-1995 7.09e-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: 41.54  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1648 PSNLQIIIKELLSMHHQPDPALTKE----FDYLPPV-----DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS 1718
Cdd:cd02669     71 PDNYEIIDSSLDDIKYVLNPTYTKEqisdLDRDPKLsrdldGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1719 V-DDDTDNPDDSVFYQVQS-LFGHLMESKL--QYYVPENFWKIFKMW-NKELYVREQQDAYEFFTSLIDQMDEYLKKMGR 1793
Cdd:cd02669    151 YeNYENIKDRKSELVKRLSeLIRKIWNPRNfkGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKK 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1794 D--QIFKNTFQG---IYSdQKIckdcPHRYEREEAFMALNLGVTSCQS-----LEISLD-----------------QFVR 1846
Cdd:cd02669    231 PnsSIIHDCFQGkvqIET-QKI----KPHAEEEGSKDKFFKDSRVKKTsvspfLLLTLDlpppplfkdgneeniipQVPL 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265894 1847 GEVLEGsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFgfdwESGRSIKYDEQ--IRFPWMLNMEPYTVSGMARQDS 1924
Cdd:cd02669    306 KQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRF----SKNNFFKEKNPtiVNFPIKNLDLSDYVHFDKPSLN 378
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217265894 1925 SSevgengrsvdqggggsprkkvaltENYELVGVIVHSGQAH-AGHYYSFIKDRrgcGKGKWYKFNDTVIEE 1995
Cdd:cd02669    379 LS------------------------TKYNLVANIVHEGTPQeDGTWRVQLRHK---STNKWFEIQDLNVKE 423
Ubl_AtNPL4_like cd17055
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ...
968-1029 9.41e-03

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


Pssm-ID: 340575  Cd Length: 73  Bit Score: 37.19  E-value: 9.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217265894  968 TKD-TFTVEAHSNETIGSVRWKIAKQLCSPVDNIQI--FTNDSLLTvNKDQKLLHQLGFSDEQIL 1029
Cdd:cd17055      7 SRDgTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLslDPGPDLLT-AKSSATLSQLGLKHGDMV 70
 
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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