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Conserved domains on  [gi|2217294109|ref|XP_047286211|]
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sacsin isoform X3 [Homo sapiens]

Protein Classification

HEPN domain-containing protein( domain architecture ID 13018383)

HEPN (higher eukarytoes and prokaryotes nucleotide)-binding domain-containing protein may be involved in nucleotide binding; similar to Homo sapiens sacsin, a 520-kDa protein mutated in the early-onset neurodevelopmental and neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_Sacsin cd17049
ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ ...
 15-86 6.58e-34

ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ homolog subfamily C member 29 (DNAJC29), is encoded by SACS gene that is highly expressed in the brain. Mutations in SACS can cause the neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix Saguenay (ARSACS) which is characterized by early-onset spastic ataxia. Sacsin is a modular protein that is localized on the mitochondrial surface and possibaly required for normal mitochondrial network organization. Sacsin knockdown resulted in a reduction in cells expressing plyglutamine-expanded ataxin-1, which correlated with a loss of cells with large nuclear ataxin-1 incusions. At the N-terminus, sacsin contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which can interact with the proteasome. At the C-terminus, sacsin harbors a protein-protein interaction J-domain followed by an higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain. The J-domain is typically associated with DnaJ-like co-chaperones involved in regulation of the Hsp70 heat shock system.


:

Pssm-ID: 340569  Cd Length: 73  Bit Score: 126.28  E-value: 6.58e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217294109   15 RWVPVTVLPGCVGCRTVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIG-DLTSKNCHLFVNL 86
Cdd:cd17049      1 RLPRVTVLHEYIGCRTFEVPPSAAVRDIKELIYEETDFPVSEQQLWHNGKELSDWVKIGgLVPSGSHEIFLTL 73
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
4459-4575 4.46e-22

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


:

Pssm-ID: 214800  Cd Length: 113  Bit Score: 94.29  E-value: 4.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109  4459 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDKDVKPTALAQKIEEYSQQLEGLTNDVHTLEAYG 4538
Cdd:smart00748    1 LRRAKRFLEAAKLDLEKGFYDLAAFLSQQAAELALKALLLALGGEPPKTHSLRELLSELEKLLRLPEFIDEIRECLNLLE 80

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2217294109  4539 VDSLKTRYPDLLPfpqiPNDRFTSEVAMRVMECTACI 4575
Cdd:smart00748   81 EAYIKSRYPDAGE----PLEWYTKEDAEELLKCAEEI 113
DnaJ super family cl02542
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4330-4365 1.06e-03

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


The actual alignment was detected with superfamily member pfam00226:

Pssm-ID: 413365 [Multi-domain]  Cd Length: 63  Bit Score: 40.15  E-value: 1.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2217294109 4330 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKHLQN 4365
Cdd:pfam00226   14 DEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINE 48
 
Name Accession Description Interval E-value
Ubl_Sacsin cd17049
ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ ...
 15-86 6.58e-34

ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ homolog subfamily C member 29 (DNAJC29), is encoded by SACS gene that is highly expressed in the brain. Mutations in SACS can cause the neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix Saguenay (ARSACS) which is characterized by early-onset spastic ataxia. Sacsin is a modular protein that is localized on the mitochondrial surface and possibaly required for normal mitochondrial network organization. Sacsin knockdown resulted in a reduction in cells expressing plyglutamine-expanded ataxin-1, which correlated with a loss of cells with large nuclear ataxin-1 incusions. At the N-terminus, sacsin contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which can interact with the proteasome. At the C-terminus, sacsin harbors a protein-protein interaction J-domain followed by an higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain. The J-domain is typically associated with DnaJ-like co-chaperones involved in regulation of the Hsp70 heat shock system.


Pssm-ID: 340569  Cd Length: 73  Bit Score: 126.28  E-value: 6.58e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217294109   15 RWVPVTVLPGCVGCRTVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIG-DLTSKNCHLFVNL 86
Cdd:cd17049      1 RLPRVTVLHEYIGCRTFEVPPSAAVRDIKELIYEETDFPVSEQQLWHNGKELSDWVKIGgLVPSGSHEIFLTL 73
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
4459-4575 4.46e-22

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


Pssm-ID: 214800  Cd Length: 113  Bit Score: 94.29  E-value: 4.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109  4459 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDKDVKPTALAQKIEEYSQQLEGLTNDVHTLEAYG 4538
Cdd:smart00748    1 LRRAKRFLEAAKLDLEKGFYDLAAFLSQQAAELALKALLLALGGEPPKTHSLRELLSELEKLLRLPEFIDEIRECLNLLE 80

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2217294109  4539 VDSLKTRYPDLLPfpqiPNDRFTSEVAMRVMECTACI 4575
Cdd:smart00748   81 EAYIKSRYPDAGE----PLEWYTKEDAEELLKCAEEI 113
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
4459-4585 3.56e-06

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


Pssm-ID: 441851  Cd Length: 121  Bit Score: 48.79  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109 4459 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDK--DVkpTALAQKIEEYSQQLEGLTNDVHTLEA 4536
Cdd:COG2250      1 LRRAERDLEAAELLLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKthDL--RELLELLEKLLPEPEELRDLLRLLDK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2217294109 4537 YGVDSlktRYPDLLPfpqIPNDRFTSEVAMRVMECTACIIIKLENFMQQ 4585
Cdd:COG2250     79 AYIPA---RYPDALP---EGPEEYTREEAEEALELAEEVLEFVEKLLKE 121
HEPN pfam05168
HEPN domain;
4455-4572 3.96e-06

HEPN domain;


Pssm-ID: 398711  Cd Length: 117  Bit Score: 48.77  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109 4455 ARRWLRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAAdYAVRGKSDK---DVkpTALAQKIEEYSQQLEGLTNDV 4531
Cdd:pfam05168    1 AEDWLRRAEEDLEAAELLLEEGDYDWACFHAQQAAEKALKAL-LLKLGGDPPkthDL--RELLGELKKGLGLPEELREIL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217294109 4532 HTLEAYGVDSlktRYPDLLPfpqipndrFTSEVAMRVMECT 4572
Cdd:pfam05168   78 DELEKAYIES---RYPDADE--------GTEEDAEEALKDA 107
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 30-75 8.70e-05

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 43.31  E-value: 8.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217294109   30 TVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIGDL 75
Cdd:pfam00240   12 TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEY 57
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4330-4365 1.06e-03

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 40.15  E-value: 1.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2217294109 4330 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKHLQN 4365
Cdd:pfam00226   14 DEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINE 48
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4330-4368 1.68e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 39.53  E-value: 1.68e-03
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 2217294109  4330 ESERKKIIRRLYLKWHPDKNPENHDIANEVFKhlqnEIN 4368
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEEAEEKFK----EIN 49
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 4317-4378 1.76e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.03  E-value: 1.76e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217294109 4317 EVTSVVEQAWKlpeSERKKIIRRLYLKWHPDKNPENHDI------ANEVFKHLQNEinrlEKQAFLDQ 4378
Cdd:PRK14281     7 EVLGVSRSADK---DEIKKAYRKLALKYHPDKNPDNKEAeehfkeVNEAYEVLSND----DKRRRYDQ 67
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 36-68 1.78e-03

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 39.93  E-value: 1.78e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217294109    36 SWTVRDVKERIFAETGFPVSEQRLWRGGRELSD 68
Cdd:smart00213   20 SDTVSELKEKIAELTGIPPEQQRLIYKGKVLED 52
 
Name Accession Description Interval E-value
Ubl_Sacsin cd17049
ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ ...
 15-86 6.58e-34

ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ homolog subfamily C member 29 (DNAJC29), is encoded by SACS gene that is highly expressed in the brain. Mutations in SACS can cause the neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix Saguenay (ARSACS) which is characterized by early-onset spastic ataxia. Sacsin is a modular protein that is localized on the mitochondrial surface and possibaly required for normal mitochondrial network organization. Sacsin knockdown resulted in a reduction in cells expressing plyglutamine-expanded ataxin-1, which correlated with a loss of cells with large nuclear ataxin-1 incusions. At the N-terminus, sacsin contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which can interact with the proteasome. At the C-terminus, sacsin harbors a protein-protein interaction J-domain followed by an higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain. The J-domain is typically associated with DnaJ-like co-chaperones involved in regulation of the Hsp70 heat shock system.


Pssm-ID: 340569  Cd Length: 73  Bit Score: 126.28  E-value: 6.58e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217294109   15 RWVPVTVLPGCVGCRTVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIG-DLTSKNCHLFVNL 86
Cdd:cd17049      1 RLPRVTVLHEYIGCRTFEVPPSAAVRDIKELIYEETDFPVSEQQLWHNGKELSDWVKIGgLVPSGSHEIFLTL 73
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
4459-4575 4.46e-22

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


Pssm-ID: 214800  Cd Length: 113  Bit Score: 94.29  E-value: 4.46e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109  4459 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDKDVKPTALAQKIEEYSQQLEGLTNDVHTLEAYG 4538
Cdd:smart00748    1 LRRAKRFLEAAKLDLEKGFYDLAAFLSQQAAELALKALLLALGGEPPKTHSLRELLSELEKLLRLPEFIDEIRECLNLLE 80

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2217294109  4539 VDSLKTRYPDLLPfpqiPNDRFTSEVAMRVMECTACI 4575
Cdd:smart00748   81 EAYIKSRYPDAGE----PLEWYTKEDAEELLKCAEEI 113
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 19-84 9.16e-08

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.83  E-value: 9.16e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217294109   19 VTVLPGCVGCRTVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIGDL-TSKNCHLFV 84
Cdd:cd17039      1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYgIKDGSTIHL 67
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
4459-4585 3.56e-06

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


Pssm-ID: 441851  Cd Length: 121  Bit Score: 48.79  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109 4459 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDK--DVkpTALAQKIEEYSQQLEGLTNDVHTLEA 4536
Cdd:COG2250      1 LRRAERDLEAAELLLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKthDL--RELLELLEKLLPEPEELRDLLRLLDK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2217294109 4537 YGVDSlktRYPDLLPfpqIPNDRFTSEVAMRVMECTACIIIKLENFMQQ 4585
Cdd:COG2250     79 AYIPA---RYPDALP---EGPEEYTREEAEEALELAEEVLEFVEKLLKE 121
HEPN pfam05168
HEPN domain;
4455-4572 3.96e-06

HEPN domain;


Pssm-ID: 398711  Cd Length: 117  Bit Score: 48.77  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217294109 4455 ARRWLRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAAdYAVRGKSDK---DVkpTALAQKIEEYSQQLEGLTNDV 4531
Cdd:pfam05168    1 AEDWLRRAEEDLEAAELLLEEGDYDWACFHAQQAAEKALKAL-LLKLGGDPPkthDL--RELLGELKKGLGLPEELREIL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217294109 4532 HTLEAYGVDSlktRYPDLLPfpqipndrFTSEVAMRVMECT 4572
Cdd:pfam05168   78 DELEKAYIES---RYPDADE--------GTEEDAEEALKDA 107
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 30-75 8.70e-05

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 43.31  E-value: 8.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217294109   30 TVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIGDL 75
Cdd:pfam00240   12 TLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEY 57
Ubl_FUBI cd01793
ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is ...
 30-74 9.39e-04

ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is a pro-apoptotic regulatory gene FAU encoding ubiquitin-like protein with ribosomal protein S30 as a C-terminal extension. FUBI functions as a tumor suppressor protein that may be involved in the ATP-dependent proteolytic activity of ubiquitin. The N-terminal ubiquitin-like (Ubl) domain of FUBI has the beta-grasp Ubl fold, and it may act as a substitute or an inhibitor of ubiquitin or one of ubiquitin's close relatives UCRP, FAT10, and Nedd8.


Pssm-ID: 340491  Cd Length: 74  Bit Score: 40.73  E-value: 9.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217294109   30 TVAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIGD 74
Cdd:cd01793     12 TLEVSGNETVADIKAHIAALEGIAVEDQVLLYAGAPLEDDVVLGQ 56
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4330-4365 1.06e-03

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 40.15  E-value: 1.06e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2217294109 4330 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKHLQN 4365
Cdd:pfam00226   14 DEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINE 48
Ubl_AtUPL5_like cd16107
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) ...
 31-68 1.15e-03

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) and similar proteins; Arabidopsis thaliana AtUPL5, also termed HECT-type E3 ubiquitin transferase UPL5, is an E3 ubiquitin-protein ligase that contains a ubiquitin-like domain (Ubl), a C-type lectin-binding domain, a leucine zipper and a HECT domain. HECT domain containing-ubiquitin-protein ligases have more than one member in different genomes, these proteins have been classified into four sub-families (UPL1/2, UPL3/4, UPL5 and UPL6/7). AtUPL5 fUPL5 regulates leaf senescence in Arabidopsis through degradation of the transcription factor WRKY53.


Pssm-ID: 340524  Cd Length: 70  Bit Score: 40.18  E-value: 1.15e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217294109   31 VAALASWTVRDVKERIFAETGFPVSEQRLWRGGRELSD 68
Cdd:cd16107     14 LHAKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQH 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4330-4368 1.68e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 39.53  E-value: 1.68e-03
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 2217294109  4330 ESERKKIIRRLYLKWHPDKNPENHDIANEVFKhlqnEIN 4368
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEEAEEKFK----EIN 49
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 4317-4378 1.76e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.03  E-value: 1.76e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217294109 4317 EVTSVVEQAWKlpeSERKKIIRRLYLKWHPDKNPENHDI------ANEVFKHLQNEinrlEKQAFLDQ 4378
Cdd:PRK14281     7 EVLGVSRSADK---DEIKKAYRKLALKYHPDKNPDNKEAeehfkeVNEAYEVLSND----DKRRRYDQ 67
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 36-68 1.78e-03

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 39.93  E-value: 1.78e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217294109    36 SWTVRDVKERIFAETGFPVSEQRLWRGGRELSD 68
Cdd:smart00213   20 SDTVSELKEKIAELTGIPPEQQRLIYKGKVLED 52
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 4330-4378 2.69e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 43.63  E-value: 2.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217294109 4330 ESERKKIIRRLYLKWHPDKNPENHDIANEVFKHLQNEINRL---EKQAFLDQ 4378
Cdd:PRK14282    18 QEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLsdpQKRAMYDR 69
Ubl_parkin cd01798
ubiquitin-like (Ubl) domain found in parkin and similar proteins; Parkin, also termed ...
 35-82 5.23e-03

ubiquitin-like (Ubl) domain found in parkin and similar proteins; Parkin, also termed Parkinson juvenile disease protein 2, is a RBR-type E3 ubiquitin-protein ligase that is associated with recessive early onset Parkinson's disease (PD), and exerts a protective effect against dopamine-induced alpha-synuclein-dependent cell toxicity. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Parkin functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. It mediates monoubiquitination as well as Lys-6-, Lys-11-, Lys-48- and Lys-63-linked polyubiquitination of substrates depending on the context. Parkin may enhance cell viability and protects dopaminergic neurons from oxidative stress-mediated death by regulating mitochondrial function. It also limits the production of reactive oxygen species (ROS), and regulates cyclin-E during neuronal apoptosis. Moreover, parkin displays a ubiquitin ligase-independent function in transcriptional repression of p53. Parkin contains an N-terminal ubiquitin-like (Ubl) domain and a C-terminal RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction.


Pssm-ID: 340496  Cd Length: 74  Bit Score: 38.43  E-value: 5.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217294109   35 ASWTVRDVKERIFAETGFPVSEQRLWRGGRELSDwikigDLTSKNCHL 82
Cdd:cd01798     17 SDWSILQLKEVVAKRQGVPPDQLRIIFAGKELSD-----DLTLQNCDL 59
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4330-4368 5.62e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 42.44  E-value: 5.62e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217294109 4330 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKhlqnEIN 4368
Cdd:PRK10767    18 EDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFK----EIK 51
Ubl_UBTD cd01794
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and ...
 38-74 9.12e-03

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins; This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340492  Cd Length: 69  Bit Score: 37.65  E-value: 9.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217294109   38 TVRDVKERIFAETGFPVSEQRLWRGGRELSDWIKIGD 74
Cdd:cd01794     20 TVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIED 56
 
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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