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Conserved domains on  [gi|1034557138|ref|XP_016856320|]
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ubiquitin carboxyl-terminal hydrolase 24 isoform X1 [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 ...
1707-2064 5.54e-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: 5.54e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1707 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1783
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1784 KELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1863
Cdd:cd02659     79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1864 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVSGMARQ 1943
Cdd:cd02659    159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1944 DsssevgengrsvdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2023
Cdd:cd02659    239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1034557138 2024 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2064
Cdd:cd02659    297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
975-1053 1.64e-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: 1.64e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034557138  975 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQILTVK 1053
Cdd:cd17065      1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
UBA_UBP24 cd14286
UBA domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; ...
6-42 1.42e-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: 1.42e-17
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1034557138    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 ...
1707-2064 5.54e-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: 5.54e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1707 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1783
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1784 KELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1863
Cdd:cd02659     79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1864 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVSGMARQ 1943
Cdd:cd02659    159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1944 DsssevgengrsvdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2023
Cdd:cd02659    239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1034557138 2024 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2064
Cdd:cd02659    297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1709-2059 2.02e-66

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 228.10  E-value: 2.02e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1709 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1783
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1784 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---RDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1854
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1855 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1934
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1935 YTVSGMArqdsssevgengrsvdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 2014
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034557138 2015 EEFDLNDETLEyecfggeyrpkvydqtnpytdvrrryWNAYMLFY 2059
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
975-1053 1.64e-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: 1.64e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034557138  975 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQILTVK 1053
Cdd:cd17065      1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1701-2161 1.35e-39

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 161.96  E-value: 1.35e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1701 DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1780
Cdd:COG5077    186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1781 MWNKELYVReQQDAYEFFTSLIDQMDeylKKMgRDQIFKNTFQGI---YSDQKI-CKDCPHRYEREEAFMALNLGVTSCQ 1856
Cdd:COG5077    264 GWDSDDSFM-QHDIQEFNRVLQDNLE---KSM-RGTVVENALNGIfvgKMKSYIkCVNVNYESARVEDFWDIQLNVKGMK 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1857 SLEISLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEP 1934
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLP 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1935 YTvsgmarqDSSSEVGENGRSVdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVI 2014
Cdd:COG5077    416 FL-------DRDADKSENSDAV-----------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRV 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 2015 EEFDLNdETLEyECFGGE--YRPKVYDQTNPytdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPS 2092
Cdd:COG5077    469 TRATEK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVA 522
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034557138 2093 SPEISPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2161
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 1.42e-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: 1.42e-17
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1034557138    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 ...
1707-2064 5.54e-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: 5.54e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1707 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV---FYQVQSLFGHLMESKLQYYVPenFWKIFKMWN 1783
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSvplALQRLFLFLQLSESPVKTTEL--TDKTRSFGW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1784 KELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLD 1863
Cdd:cd02659     79 DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1864 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVSGMARQ 1943
Cdd:cd02659    159 AYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1944 DsssevgengrsvdqgggGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDet 2023
Cdd:cd02659    239 E-----------------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD---DGKWYKFNDDVVTPFDPND-- 296
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1034557138 2024 LEYECFGGEYRPKVYDQTNpytDVRRRYWNAYMLFYQRVSD 2064
Cdd:cd02659    297 AEEECFGGEETQKTYDSGP---RAFKRTTNAYMLFYERKSP 334
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1709-2059 2.02e-66

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 228.10  E-value: 2.02e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1709 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDN----PDDSVFYQVQSLFGHL-MESKLQYYVPENFWKIFKMWN 1783
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrynKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1784 KELYVREQQDAYEFFTSLIDQMDEYLKKMG---RDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMAL------NLGVTS 1854
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHsteNESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLslpipgDSAELK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1855 CQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESgrSIKYDEQIRFPWMLNMEP 1934
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1935 YTVSGMArqdsssevgengrsvdqggggsprKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVI 2014
Cdd:pfam00443  239 YLAEELK------------------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAY---ENNRWYKFDDEKV 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034557138 2015 EEFDLNDETLEyecfggeyrpkvydqtnpytdvrrryWNAYMLFY 2059
Cdd:pfam00443  292 TEVDEETAVLS--------------------------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1710-2060 1.39e-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: 206.57  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvr 1789
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1790 eQQDAYEFFTSLIDQMDEYLKKMGR--------DQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGV----TSCQS 1857
Cdd:cd02257     22 -QQDAHEFLLFLLDKLHEELKKSSKrtsdssslKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVS 100
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1858 LEISLDQFVRGEVLEGSNAYYCEKCKeKRITVKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTV 1937
Cdd:cd02257    101 LEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPYLS 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1938 SGMARQDSSSEVGengrsvdqggggsprkkvalteNYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFNDTVIEE 2016
Cdd:cd02257    179 EGEKDSDSDNGSY----------------------KYELVAVVVHSGTsADSGHYVAYVKDP---SDGKWYKFNDDKVTE 233
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1034557138 2017 FDLNDEtleyecfggeyrpkvydqtnpyTDVRRRYWNAYMLFYQ 2060
Cdd:cd02257    234 VSEEEV----------------------LEFGSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2059 8.01e-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: 8.01e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS-----------VFYQVQSLFGHLMESKLQYYVPENFWKI 1778
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepqtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1779 FkmwnkELYVREQQDAYEF---FTSLIDqmDEYLKKMGRD--QIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVT 1853
Cdd:cd02668     81 L-----GLDTGQQQDAQEFsklFLSLLE--AKLSKSKNPDlkNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1854 SCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNME 1933
Cdd:cd02668    154 GHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1934 PYtvsgMARQDSSSEVgengrsvdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRRgcgKGKWYKFNDT 2012
Cdd:cd02668    234 EY----LAESDEGSYV------------------------YELSGVLIHQGVsAYSGHYIAHIKDEQ---TGEWYKFNDE 282
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034557138 2013 VIEE-----FDLNDETLEYECFGGEYRPKVYDQTnpytdvrrrywNAYMLFY 2059
Cdd:cd02668    283 DVEEmpgkpLKLGNSEDPAKPRKSEIKKGTHSSR-----------TAYMLVY 323
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2059 1.02e-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: 1.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDS--VFYQVQSLFGHLMESKLQYYVPENFWKIFKMWNKELY 1787
Cdd:cd02661      3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1788 VREQQDAYEFFTSLIDQM-----DEYLKKMGRDQIFKNT------FQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQ 1856
Cdd:cd02661     83 IGRQEDAHEFLRYLLDAMqkaclDRFKKLKAVDPSSQETtlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1857 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFdwesGRSIKYDEQIRFPWMLNMEPYt 1936
Cdd:cd02661    163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN----FRGGKINKQISFPETLDLSPY- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1937 vsgmarqdsssevgengrsVDQGGGGSPRkkvaltenYELVGVIVHSG-QAHAGHYYSFIKDRRgcgkGKWYKFNDTVIE 2015
Cdd:cd02661    238 -------------------MSQPNDGPLK--------YKLYAVLVHSGfSPHSGHYYCYVKSSN----GKWYNMDDSKVS 286
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1034557138 2016 EFDLNDetleyecfggeyrpkVYDQtnpytdvrrrywNAYMLFY 2059
Cdd:cd02661    287 PVSIET---------------VLSQ------------KAYILFY 303
Ubl_UBP24 cd17065
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ...
975-1053 1.64e-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: 1.64e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034557138  975 FHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQILTVK 1053
Cdd:cd17065      1 FHGHPLTLHVTCESTKQEFTLEVHSNETLGSVRQKIAERLNCPVDQVQIFANEKLLPSNKDQKLLHQLGFTDEQILTVK 79
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2059 6.12e-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: 6.12e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSV--------------FYQVQSLFGHLMESKLQyyvpeNF 1775
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsclscamdeifqeFYYSGDRSPYGPINLLY-----LS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1776 WKIfkmwNKELYVREQQDAYEFFTSLIDQM--------DEYLKKMGRDQIFKNTFQGIYSDQKICKDCPHRYEREEAFMA 1847
Cdd:cd02660     77 WKH----SRNLAGYSQQDAHEFFQFLLDQLhthyggdkNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLD 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1848 LNL---------------GVTSCQSLEISLDQFVRGEVLeGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDw 1912
Cdd:cd02660    153 LSLdipnkstpswalgesGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS- 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1913 ESGRSIKYDEQIRFPWMLNMEPYTVSGMARQDSSSEVgengrsvdqggggSPRKKvaltenYELVGVIVHSGQAHAGHYY 1992
Cdd:cd02660    231 LNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSL-------------DPDYT------YDLFAVVVHKGTLDTGHYT 291
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034557138 1993 SFIKDrrgcGKGKWYKFNDTVIEEFDLNDetleyecfggeyrpkVYDQtnpytdvrrrywNAYMLFY 2059
Cdd:cd02660    292 AYCRQ----GDGQWFKFDDAMITRVSEEE---------------VLKS------------QAYLLFY 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1701-2161 1.35e-39

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 161.96  E-value: 1.35e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1701 DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPEnFWKIFk 1780
Cdd:COG5077    186 NSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTGEEPVDTTE-LTRSF- 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1781 MWNKELYVReQQDAYEFFTSLIDQMDeylKKMgRDQIFKNTFQGI---YSDQKI-CKDCPHRYEREEAFMALNLGVTSCQ 1856
Cdd:COG5077    264 GWDSDDSFM-QHDIQEFNRVLQDNLE---KSM-RGTVVENALNGIfvgKMKSYIkCVNVNYESARVEDFWDIQLNVKGMK 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1857 SLEISLDQFVRGEVLEGSNAYYCEK--CKEKRitvKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEP 1934
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAK---KGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLP 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1935 YTvsgmarqDSSSEVGENGRSVdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVI 2014
Cdd:COG5077    416 FL-------DRDADKSENSDAV-----------------YVLYGVLVHSGDLHEGHYYALLKPEK---DGRWYKFDDTRV 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 2015 EEFDLNdETLEyECFGGE--YRPKVYDQTNPytdvrRRYWNAYMLFYqrvsdqnspvlpkksrvsvVRQEAEDLSLSAPS 2092
Cdd:COG5077    469 TRATEK-EVLE-ENFGGDhpYKDKIRDHSGI-----KRFMSAYMLVY-------------------LRKSMLDDLLNPVA 522
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034557138 2093 SPEISPQSSPRphrpnndrlsiLTKLVKKGEKKGLfvEKMPARIYQMVRDENLKFMKNRDVYssDYFSF 2161
Cdd:COG5077    523 AVDIPPHVEEV-----------LSEEIDKTEVRCK--EIDEIHLYRGVRLYTIDSFIHYHGF--DYPDF 576
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2060 7.07e-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: 145.53  E-value: 7.07e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYmqpglpesllsvdddtdnpDDSVFYQVQSLFGHLMESKLQYYV--PENFWKIFKMWNKELY 1787
Cdd:cd02663      1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENELFD 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1788 VREQQDAYEFFTSLIDQMDEYLKK------MGRDQIFKNT-----------FQGIYSDQKICKDCPHRYEREEAFMALNL 1850
Cdd:cd02663     62 NYMHQDAHEFLNFLLNEIAEILDAerkaekANRKLNNNNNaepqptwvheiFQGILTNETRCLTCETVSSRDETFLDLSI 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1851 GVTSCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWML 1930
Cdd:cd02663    142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1931 NMEpytvsgmarqdSSSEVGENgrsvdqggggsprkkvaLTENYELVGVIVHSGQ-AHAGHYYSFIKDrrgcgKGKWYKF 2009
Cdd:cd02663    222 RLF-----------NTTDDAEN-----------------PDRLYELVAVVVHIGGgPNHGHYVSIVKS-----HGGWLLF 268
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034557138 2010 NDTVIEEFDlnDETLEYecFggeyrpkVYDQTNPYTdvrrrywnAYMLFYQ 2060
Cdd:cd02663    269 DDETVEKID--ENAVEE--F-------FGDSPNQAT--------AYVLFYQ 300
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2060 1.04e-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: 1.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVfqqlymqpglpesllsvdddtdnpddsvfyqVQSLFGHlmesklqyyvpenfwkifkmwnkelyvr 1789
Cdd:cd02674      1 GLRNLGNTCYMNSI-------------------------------LQCLSAD---------------------------- 21
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1790 eQQDAYEFFTSLIDQMDeylkkmgrdQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNL------GVTSCQSLEISLD 1863
Cdd:cd02674     22 -QQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLpipsgsGDAPKVTLEDCLR 91
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1864 QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPW-MLNMEPYtvsgmar 1942
Cdd:cd02674     92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLnDLDLTPY------- 162
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1943 qdsssevgengrsVDQGGGGSPRKkvaltenYELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLNDE 2022
Cdd:cd02674    163 -------------VDTRSFTGPFK-------YDLYAVVNHYGSLNGGHYTAYCKNNE---TNDWYKFDDSRVTKVSESSV 219
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1034557138 2023 tleyecfggeyrpkvydQTNpytdvrrrywNAYMLFYQ 2060
Cdd:cd02674    220 -----------------VSS----------SAYILFYE 230
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2021 9.22e-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: 9.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENfwKIFK-MWNKELYV 1788
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD--YFLEaSRPPWFTP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1789 REQQDAYEFFTSLIDQMDEYLKKMgrdqifkntFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLeisLDQFVRG 1868
Cdd:cd02664     79 GSQQDCSEYLRYLLDRLHTLIEKM---------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL---LNYFLSP 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1869 EVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMepyTVSGMARQDSSSE 1948
Cdd:cd02664    147 EKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSL---PVRVESKSSESPL 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1949 VGENGRSVDQGGGgsprkkVALTENYELVGVIVHSG-QAHAGHYYSF---IKDRRGCGK--------------GKWYKFN 2010
Cdd:cd02664    224 EKKEEESGDDGEL------VTRQVHYRLYAVVVHSGySSESGHYFTYardQTDADSTGQecpepkdaeendesKNWYLFN 297
                          330
                   ....*....|.
gi 1034557138 2011 DTVIEEFDLND 2021
Cdd:cd02664    298 DSRVTFSSFES 308
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2060 1.92e-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: 1.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDtdnpddsvfyqvqsLFGHLMESKLQYyvpenfwKIFKmwnkelyvr 1789
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE--------------LFSQVCRKAPQF-------KGYQ--------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1790 eQQDAYEFFTSLIDQMDEYLkkmgrDQIFKntfqGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEIS----LDQF 1865
Cdd:cd02667     51 -QQDSHELLRYLLDGLRTFI-----DSIFG----GELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECSiescLKQF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1866 VRGEVLEGSNAYYCEKCKEKRitvKRTCIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLNMEPYTvsgmarqDS 1945
Cdd:cd02667    121 TEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFC-------DP 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1946 SSEVGENGRSVdqggggsprkkvalteNYELVGVIVHSGQAHAGHYYSFIKDR------------------RGCGKGKWY 2007
Cdd:cd02667    190 KCNSSEDKSSV----------------LYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeAGPGSGQWY 253
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034557138 2008 KFNDTVIEEFDLnDETLEYEcfggeyrpkvydqtnpytdvrrrywnAYMLFYQ 2060
Cdd:cd02667    254 YISDSDVREVSL-EEVLKSE--------------------------AYLLFYE 279
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2012 6.60e-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: 6.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYmqpGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLmeSKL-------QYYVPENFW------ 1776
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLF---SIPSFQWRYDDLENKFPSDVVDPANDLNCQL--IKLadgllsgRYSKPASLKsendpy 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1777 ------KIFKM----WNKELYVREQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIysDQKI-CKDCPHRY--EREE 1843
Cdd:cd02658     76 qvgikpSMFKAligkGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPNDLFKFMI--EDRLeCLSCKKVKytSELS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1844 AFMALNL------------GVTSCQSLEISLDQFVRGEVLEgsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGF- 1910
Cdd:cd02658    154 EILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLl 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1911 -DWesgRSIKYDEQIRFPWMLnmepytvsgmarqdsssevgengrsvdqGGGgsprkkvalteNYELVGVIVHSG-QAHA 1988
Cdd:cd02658    230 eNW---VPKKLDVPIDVPEEL----------------------------GPG-----------KYELIAFISHKGtSVHS 267
                          330       340
                   ....*....|....*....|....
gi 1034557138 1989 GHYYSFIKdRRGCGKGKWYKFNDT 2012
Cdd:cd02658    268 GHYVAHIK-KEIDGEGKWVLFNDE 290
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2011 1.37e-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: 1.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQV---QSLFGHlMESKLQYYVPENFWKIF------- 1779
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTnalRDLFDT-MDKKQEPVPPIEFLQLLrmafpqf 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1780 -KMWNKELYvrEQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTFQGIYSDQKI-CKDCPHRYE---REEAFMALNLGVTS 1854
Cdd:cd02657     80 aEKQNQGGY--AQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMkCTESPDEEEvstESEYKLQCHISITT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1855 -CQSLEISLDQFVRGEVLEGSnayycEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNM- 1932
Cdd:cd02657    158 eVNYLQDGLKKGLEEEIEKHS-----PTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLy 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1933 EPYTVSGMarqdsssevgengrsvdqggggsprkkvaltenYELVGVIVHSGQ-AHAGHYYSFIKDRrgcGKGKWYKFND 2011
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 1.42e-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: 1.42e-17
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1034557138    6 EQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLT 42
Cdd:cd14286      1 EEHVTTLLCMGFSDPEEIRKALRLAKNDLNEAVAILT 37
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1683-2018 7.75e-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: 7.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1683 HHQPDPALTkefdyLPPVDSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDdsvfyQVQSLFGHL 1762
Cdd:cd02671      4 VPAPQPSSA-----TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVE-----QLQSSFLLN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1763 ME---SKLQYYVPENFWKIFKMWNKELYVREQQDAYEFFTSLIDQMDEYLKKMgrdqifkntFQGIYSDQKICKDCPHRY 1839
Cdd:cd02671     74 PEkynDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKD---------FQGQLVLRTRCLECETFT 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1840 EREEAFMALNLGV------TSCQSLEISLD-------------QFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSV 1900
Cdd:cd02671    145 ERREDFQDISVPVqeselsKSEESSEISPDpktemktlkwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEV 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1901 LVIHLMRFG-----FDWESGRSiKYDEQIRFPWMLNMEpytvsgmarqdsssevgengrsvdqGGGGSPRKKValtenYE 1975
Cdd:cd02671    225 ITIHLKCFAangseFDCYGGLS-KVNTPLLTPLKLSLE-------------------------EWSTKPKNDV-----YR 273
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1034557138 1976 LVGVIVHSG-QAHAGHYYSFIkdrrgcgkgKWYKFNDT---VIEEFD 2018
Cdd:cd02671    274 LFAVVMHSGaTISSGHYTAYV---------RWLLFDDSevkVTEEKD 311
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2060 7.78e-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: 7.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQPGLPESLLSVdddtdnpddsvfyqvqslfghlmesklqyyvpenfwkifkmwnkelyvR 1789
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------L 32
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1790 EQQDAYEFFTSLIDQMdeylkkmgrDQIFKNTFQGIYSDQKICKDCPHRYE-REEAFMALNLGV-----TSCQSLEISLD 1863
Cdd:cd02662     33 EQQDAHELFQVLLETL---------EQLLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVpnqssGSGTTLEHCLD 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1864 QFVRGEVLEGsnaYYCEKCKEKritvkrtcIKSLPSVLVIHLMRFGFDwESGRSIKYDEQIRFPWMLnmepytvsgmarq 1943
Cdd:cd02662    104 DFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERL------------- 158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1944 dsssevgengrsvdqggggsPRKKvaltenYELVGVIVHSGQAHAGHYYSF-----------------IKDRRGCGKGKW 2006
Cdd:cd02662    159 --------------------PKVL------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrMREGPSSTSHPW 212
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034557138 2007 YKFNDTVIEEFDLNDETLEYEcfggeyrpkvydqtnpytdvrrrywnAYMLFYQ 2060
Cdd:cd02662    213 WRISDTTVKEVSESEVLEQKS--------------------------AYMLFYE 240
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
1709-2014 9.38e-14

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 74.61  E-value: 9.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1709 VGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENFWKIFKMW--NKEL 1786
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1787 ----YVREQQDAyEFFTSLI--------DQM-DEYLKKMGRDQ----IFKNTFQGIYSDQKICKDCPHRYEREEAFMALN 1849
Cdd:pfam13423   81 glldEDRETNSA-ISLSSLIqsfnrfllDQLsSEENSTPPNPSpaesPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1850 L--------------GVTSCQSLEISLDQfvrgevlEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESG 1915
Cdd:pfam13423  160 LiyprkpssnnkkppNQTFSSILKSSLER-------ETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1916 RSIKydeqirfPWmLNMEPYTvsgmarqdsssevgengrSVDQGGGGSPRKKValtenYELVGVIVH-SGQAHAGHYYSF 1994
Cdd:pfam13423  233 WKTP-------GW-LPPEIGL------------------TLSDDLQGDNEIVK-----YELRGVVVHiGDSGTSGHLVSF 281
                          330       340
                   ....*....|....*....|....
gi 1034557138 1995 IK----DRRGCGKGKWYKFNDTVI 2014
Cdd:pfam13423  282 VKvadsELEDPTESQWYLFNDFLV 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1857-2063 2.24e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 76.08  E-value: 2.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1857 SLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRfgFDWESGRSIKYDEQIRFPWM-LNMEPY 1935
Cdd:COG5560    676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPIDdLDLSGV 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1936 TVSGMarqdsSSEVGengrsvdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgCGKGKWYKFNDTVIE 2015
Cdd:COG5560    754 EYMVD-----DPRLI-----------------------YDLYAVDNHYGGLSGGHYTAYARN---FANNGWYLFDDSRIT 802
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034557138 2016 EFDLNDETLEyecfggeyrpkvydqtnpytdvrrrywNAYMLFYQRVS 2063
Cdd:COG5560    803 EVDPEDSVTS---------------------------SAYVLFYRRKS 823
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1710-2011 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 1034557138 1710 GLRNGGATCYMNAVFQQL-YMQPGLPESLLsvdddTDNPDDSVFYQV-----QSLFGHLMESKLQYYVPENFWKIFKMWN 1783
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILaLYLPKLDELLD-----DLSKELKVLKNVirkpePDLNQEEALKLFTALWSSKEHKVGWIPP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1784 KElyvrEQQDAYEFFTSLIDQMDEYLKKMGRDQIFKNTfqgiysdqkicKDCPHRYEREeaFMALNLGVTSCQSLEIS-- 1861
Cdd:COG5533     76 MG----SQEDAHELLGKLLDELKLDLVNSFTIRIFKTT-----------KDKKKTSTGD--WFDIIIELPDQTWVNNLkt 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1862 LDQFvrgevLEGSNAYYCEKC-------KEKRITVKR---TCIKSLPSVLVIHLMRFGFDwesGRSIKYDEQIRfpwmln 1931
Cdd:COG5533    139 LQEF-----IDNMEELVDDETgvkakenEELEVQAKQeyeVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD------ 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1932 mEPYTVSgmARQDSSSEVGENGRsvdqggggsprkkvaltenYELVGVIVHSGQAHAGHYYSFIKDrrgcgKGKWYKFND 2011
Cdd:COG5533    205 -EKFELP--VKHDQILNIVKETY-------------------YDLVGFVLHQGSLEGGHYIAYVKK-----GGKWEKAND 257
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1710-2038 2.48e-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: 2.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1710 GLRNGGATCYMNAVFQQLYMQpglpesllsvdddtdnpddsvfyqvqslfghlmesklQYYVPENFWKIFKmWnkelyvr 1789
Cdd:cd02665      1 GLKNVGNTCWFSAVIQSLFSQ-------------------------------------QQDVSEFTHLLLD-W------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1790 eQQDAYEFFTSLIDQMDEYLKKMGrdQIFKNTF--QGIYSDQKICKDcphryereEAFMALNLGVTSCQSLEISLD-QFV 1866
Cdd:cd02665     36 -LEDAFQAAAEAISPGEKSKNPMV--QLFYGTFltEGVLEGKPFCNC--------ETFGQYPLQVNGYGNLHECLEaAMF 104
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1867 RGEVlEGSNAYYCEKCKEKRITVKrtciksLPSVLVIHLMRFGFDweSGRSIKYDEQIRFPWMLNMEPYtvsgmarqdss 1946
Cdd:cd02665    105 EGEV-ELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFN--QGRPEKIHDKLEFPQIIQQVPY----------- 164
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1947 sevgengrsvdqggggsprkkvaltenyELVGVIVHSGQAHAGHYYSFIKDRRgcgKGKWYKFNDTVIEEFDLndETLEY 2026
Cdd:cd02665    165 ----------------------------ELHAVLVHEGQANAGHYWAYIYKQS---RQEWEKYNDISVTESSW--EEVER 211
                          330
                   ....*....|..
gi 1034557138 2027 ECFGGEYRPKVY 2038
Cdd:cd02665    212 DSFGGGRNPSAY 223
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
982-1052 1.33e-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: 1.33e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034557138  982 LNVTYESTKdTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLtvnKDQKLLHQLGFSDEQILTV 1052
Cdd:cd17039      1 ITVKTLDGK-TYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKEL---KDDKTLSDYGIKDGSTIHL 67
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1709-2024 6.03e-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: 6.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1709 VGLRNGGATCYMNAVFQQLYMQPGLPESLLS----------------------VDDDTDNPDDSVFYQVQSLFGHLMESK 1766
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeskaelasdypterriggreVSRSELQRSNQFVYELRSLFNDLIHSN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1767 LQYYVPEnfwkifkmwnKEL--YVREQQDAYEFFTSLIDQMDEYLK-----KMGRDQI--------FKNTFQGIYsDQKI 1831
Cdd:cd02666     82 TRSVTPS----------KELayLALRQQDVTECIDNVLFQLEVALEpisnaFAGPDTEddkeqsdlIKRLFSGKT-KQQL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1832 CKD----CPHRYEREEAFMALNLGVTSC----------QSLEISLDQFVRGEVLEgsnayycekckekritvkrtcikSL 1897
Cdd:cd02666    151 VPEsmgnQPSVRTKTERFLSLLVDVGKKgreivvllepKDLYDALDRYFDYDSLT-----------------------KL 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1898 PSVLVIHLMRFGFdwesgrsiKYDEQIrfpWMLNMEPYTVSgmarQDSSSEVGENGRSVDQGGGGSPRKKVALTEN---- 1973
Cdd:cd02666    208 PQRSQVQAQLAQP--------LQRELI---SMDRYELPSSI----DDIDELIREAIQSESSLVRQAQNELAELKHEiekq 272
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034557138 1974 --------YELVGVIVHSGQAHAGHYYSFIKDRrgcGKGKWYKFNDTVIEEFDLNDETL 2024
Cdd:cd02666    273 fddlksygYRLHAVFIHRGEASSGHYWVYIKDF---EENVWRKYNDETVTVVPASEVFL 328
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1790-2060 3.05e-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: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1790 EQQDAYEFFTSLIDQMDEYLKKMGRDqifkntfqgIYSDQKickdcphRYEREEAFMalnlgvtSCQSLEISLDQFVRGE 1869
Cdd:cd02670     22 EQQDPEEFFNFITDKLLMPLLEPKVD---------IIHGGK-------KDQDDDKLV-------NERLLQIPVPDDDDGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1870 VLEgsnayyCEKCKEKRITVKRtcIKSLPSVLVIHLMRFGfdWESGRSIKYDEQIRFPWMLNMePYTVSGMARQDS--SS 1947
Cdd:cd02670     79 GIT------LEQCLEQYFNNSV--FAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDI-PDFVADDPRACSkcQL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1948 EVGENGRSVDQGGGGSPRKKValtenyeLVGVIVHSGQA-HAGHYYSFIK--------DRRGCGKGKWYKFNDtvieefd 2018
Cdd:cd02670    148 ECRVCYDDKDFSPTCGKFKLS-------LCSAVCHRGTSlETGHYVAFVRygsyslteTDNEAYNAQWVFFDD------- 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034557138 2019 LNDetleyecfggeyRPKVYDQTNpyTDVRRRYWNAYMLFYQ 2060
Cdd:cd02670    214 MAD------------RDGVSNGFN--IPAARLLEDPYMLFYQ 241
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1856-2027 4.62e-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: 44.81  E-value: 4.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1856 QSLEISLDQFVrgevlegSNAYYCEKCKEKRITVKRTCIKSLP----SVLVIHLMRFGFDWESGRSikydeqirfpwmln 1931
Cdd:cd02672    121 QLLKRSLDLEK-------VTKAWCDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINV-------------- 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1932 mepytvsgmarQDSSSEVGENGRSVDQGGGGSPRKKVALTEN--YELVGVIVH-SGQAHAGHYYSF-IKDRRGCGKGKWY 2007
Cdd:cd02672    180 -----------VLPSGKVMQNKVSPKAIDHDKLVKNRGQESIykYELVGYVCEiNDSSRGQHNVVFvIKVNEESTHGRWY 248
                          170       180
                   ....*....|....*....|
gi 1034557138 2008 KFNDTVIEEFDLNDETLEYE 2027
Cdd:cd02672    249 LFNDFLVTPVSELAYILLYQ 268
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1707-1850 2.73e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.33  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1707 GFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS---VDDDTDNPDDSVFYQVQSLFGHLMES----KLQYYVPENFWKIF 1779
Cdd:COG5560    264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdeyEESINEENPLGMHGSVASAYADLIKQlydgNLHAFTPSGFKKTI 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1780 KMWNKELYVREQQDAYEFFTSLIDQMDEYLKKM-------------GRDQIFKNT-------------------FQGIYS 1827
Cdd:COG5560    344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIikkpytskpdlspGDDVVVKKKakecwwehlkrndsiitdlFQGMYK 423
                          170       180
                   ....*....|....*....|...
gi 1034557138 1828 DQKICKDCPHRYEREEAFMALNL 1850
Cdd:COG5560    424 STLTCPGCGSVSITFDPFMDLTL 446
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
11-41 3.69e-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: 3.69e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1034557138   11 TLLCMGFSdPATIRKALRLAKNDINEAVALL 41
Cdd:cd14297      6 QLVDMGFT-EAQARKALRKTNNNVERAVDWL 35
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1669-2016 6.97e-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: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1669 PSNLQIIIKELLSMHHQPDPALTKE----FDYLPPV-----DSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLS 1739
Cdd:cd02669     71 PDNYEIIDSSLDDIKYVLNPTYTKEqisdLDRDPKLsrdldGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1740 V-DDDTDNPDDSVFYQVQS-LFGHLMESKL--QYYVPENFWKIFKMW-NKELYVREQQDAYEFFTSLIDQMDEYLKKMGR 1814
Cdd:cd02669    151 YeNYENIKDRKSELVKRLSeLIRKIWNPRNfkGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKK 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1815 D--QIFKNTFQG---IYSdQKIckdcPHRYEREEAFMALNLGVTSCQS-----LEISLD-----------------QFVR 1867
Cdd:cd02669    231 PnsSIIHDCFQGkvqIET-QKI----KPHAEEEGSKDKFFKDSRVKKTsvspfLLLTLDlpppplfkdgneeniipQVPL 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557138 1868 GEVLEGsnaYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFgfdwESGRSIKYDEQ--IRFPWMLNMEPYTVSGMARQDS 1945
Cdd:cd02669    306 KQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRF----SKNNFFKEKNPtiVNFPIKNLDLSDYVHFDKPSLN 378
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034557138 1946 SSevgengrsvdqggggsprkkvaltENYELVGVIVHSGQAH-AGHYYSFIKDRrgcGKGKWYKFNDTVIEE 2016
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, ...
989-1050 9.58e-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: 9.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034557138  989 TKD-TFTVEAHSNETIGSVRWKIAKQLCSPVDNIQI--FTNDSLLTvNKDQKLLHQLGFSDEQIL 1050
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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