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Conserved domains on  [gi|15242392|ref|NP_196496|]
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Ubiquitin family protein [Arabidopsis thaliana]

Protein Classification

ubiquitin-like domain-containing protein( domain architecture ID 13017831)

ubiquitin family protein similar to Caldiarchaeum subterraneum Ubiquitin (Ub) which is a component of an archaeal Ub modifier system including E2 and E3 enzymes, and to uncharacterized Dictyostelium discoideum NEDD8-like protein 1 (NEDD8l1)

CATH:  3.10.20.90
Gene Ontology:  GO:0005515
PubMed:  19468686|12645912|1647207
SCOP:  4000962

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 3-72 4.61e-13

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: 57.61  E-value: 4.61e-13
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242392  3 VFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIvleVHGGTTMDDYKIKACDIFHM 72
Cdd:cd17039  1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKE---LKDDKTLSDYGIKDGSTIHL 67
 
Name Accession Description Interval E-value
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 3-72 4.61e-13

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: 57.61  E-value: 4.61e-13
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242392  3 VFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIvleVHGGTTMDDYKIKACDIFHM 72
Cdd:cd17039  1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKE---LKDDKTLSDYGIKDGSTIHL 67
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1-72 5.05e-09

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: 47.64  E-value: 5.05e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242392     1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIVLEvhgGTTMDDYKIKACDIFHM 72
Cdd:smart00213  1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLED---DRTLADYGIQDGSTIHL 69
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
1-75 6.52e-09

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 49.79  E-value: 6.52e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242392   1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIVLEvhgGTTMDDYKIKACDIFHMSDR 75
Cdd:COG5272   1 MQIFVKTLTGKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLED---DRTLADYNIQKESTLHLVTR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 3-77 1.01e-08

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: 46.78  E-value: 1.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242392    3 VFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIvLEvhGGTTMDDYKIKACDIFHMSDRMR 77
Cdd:pfam00240  1 ITVKTLDGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKV-LE--DDQTLGEYGIEDGSTIHLVLRQR 72
PTZ00044 PTZ00044
ubiquitin; Provisional
 1-79 9.78e-06

ubiquitin; Provisional


Pssm-ID: 185411 [Multi-domain]  Cd Length: 76  Bit Score: 39.42  E-value: 9.78e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242392   1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKivlEVHGGTTMDDYKIKACDIFHMSDRMRGG 79
Cdd:PTZ00044  1 MQILIKTLTGKKQSFNFEPDNTVQQVKMALQEKEGIDVKQIRLIYSGK---QMSDDLKLSDYKVVPGSTIHMVLQLRGG 76
 
Name Accession Description Interval E-value
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 3-72 4.61e-13

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: 57.61  E-value: 4.61e-13
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242392  3 VFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIvleVHGGTTMDDYKIKACDIFHM 72
Cdd:cd17039  1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKE---LKDDKTLSDYGIKDGSTIHL 67
Ubl_ubiquitin cd01803
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ...
 1-79 1.89e-09

ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains.


Pssm-ID: 340501 [Multi-domain]  Cd Length: 76  Bit Score: 48.98  E-value: 1.89e-09
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242392  1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKivlEVHGGTTMDDYKIKACDIFHMSDRMRGG 79
Cdd:cd01803  1 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGK---QLEDGRTLSDYNIQKESTLHLVLRLRGG 76
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1-72 5.05e-09

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: 47.64  E-value: 5.05e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242392     1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIVLEvhgGTTMDDYKIKACDIFHM 72
Cdd:smart00213  1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLED---DRTLADYGIQDGSTIHL 69
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
1-75 6.52e-09

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 49.79  E-value: 6.52e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242392   1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIVLEvhgGTTMDDYKIKACDIFHMSDR 75
Cdd:COG5272   1 MQIFVKTLTGKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLED---DRTLADYNIQKESTLHLVTR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 3-77 1.01e-08

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: 46.78  E-value: 1.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242392    3 VFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIvLEvhGGTTMDDYKIKACDIFHMSDRMR 77
Cdd:pfam00240  1 ITVKTLDGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKV-LE--DDQTLGEYGIEDGSTIHLVLRQR 72
PTZ00044 PTZ00044
ubiquitin; Provisional
 1-79 9.78e-06

ubiquitin; Provisional


Pssm-ID: 185411 [Multi-domain]  Cd Length: 76  Bit Score: 39.42  E-value: 9.78e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242392   1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKivlEVHGGTTMDDYKIKACDIFHMSDRMRGG 79
Cdd:PTZ00044  1 MQILIKTLTGKKQSFNFEPDNTVQQVKMALQEKEGIDVKQIRLIYSGK---QMSDDLKLSDYKVVPGSTIHMVLQLRGG 76
Ubl_FUBI cd01793
ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is ...
 1-79 5.30e-05

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: 37.26  E-value: 5.30e-05
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242392  1 MQVFIidEDGKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKiVLEvhggttmDDYKIKACDI-----FHMSDR 75
Cdd:cd01793  1 MQLFV--RAQSLHTLEVSGNETVADIKAHIAALEGIAVEDQVLLYAGA-PLE-------DDVVLGQCGIpdlatLEVAVR 70


               ....
gi 15242392 76 MRGG 79
Cdd:cd01793 71 LLGG 74
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 10-72 5.35e-05

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 37.23  E-value: 5.35e-05
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242392 10 GKKYCVEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKIVLEVHggtTMDDYKIKACDIFHM 72
Cdd:cd16106 10 GKKFTVEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEE---TLSSYKIQDGHTVHL 69
Ubl_TECR_like cd01801
ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins; ...
 2-63 5.73e-04

ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins; This family includes TECR and many TECR-like proteins, such as TECRL. TECR, also termed very-long-chain enoyl-CoA reductase, or synaptic glycoprotein SC2, or TER, or GPSN2, is a synaptic glycoprotein that catalyzes the fourth reaction in the synthesis of very long-chain fatty acids (VLCFA) which is the reduction step of the microsomal fatty acyl-elongation process. Diseases involving perturbations to normal synthesis and degradation of VLCFA (e.g. adrenoleukodystrophy and Zellweger syndrome) have significant neurological consequences. The mammalian TECR P182L mutation causes nonsyndromic mental retardation. Deletion of the yeast TECR (TSC13) homolog is lethal. TECR contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal catalytic domain. TECRL, also termed steroid 5-alpha-reductase 2-like 2 protein (SRD5A2L2), is associated with life-threatening inherited arrhythmias displaying features of both long QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT). Both TECR and TECRL contain an N-terminal Ubl domain with a beta-grasp Ubl fold, and a C-terminal catalytic domain.


Pssm-ID: 340499 [Multi-domain]  Cd Length: 77  Bit Score: 34.95  E-value: 5.73e-04
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242392  2 QVFIIDEDGKKY--CVEVEKTTTIADMKTKIYDATGmenayQYLEHRGKIVLEVHGGTTMDDYK 63
Cdd:cd01801  1 KIEVVSRKGGKQiiTLEVSSSATVADLKKAIHKKKK-----KLYPERQRLRLEVPKGKVLKDDK 59
Ubl_Rad23 cd01805
ubiquitin-like (Ubl) domain found in the Rad23 protein family; The Rad23 family includes the ...
 1-65 9.36e-04

ubiquitin-like (Ubl) domain found in the Rad23 protein family; The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry an ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. The Ubl domain is responsible for the binding to proteasome. The UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates, which suggests Rad23 proteins might be involved in certain pathways of Ub metabolism. Both the Ubl domain and the XPC-binding domain are necessary for efficient NER function of Rad23 proteins.


Pssm-ID: 340503 [Multi-domain]  Cd Length: 72  Bit Score: 34.07  E-value: 9.36e-04
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242392  1 MQVFIIDEDGKKYCVEVEKTTTIADMKTKIYDATG-MENAYQYLEHRGKIvleVHGGTTMDDYKIK 65
Cdd:cd01805  1 MKITFKTLQQQTFEIEVEPSDTVLELKEKIEQEQGdFPASGQKLIYSGKV---LKDDKTLSEYNIK 63
PRK12765 PRK12765
flagellar filament capping protein FliD;
4-35 2.02e-03

flagellar filament capping protein FliD;


Pssm-ID: 237194 [Multi-domain]  Cd Length: 595  Bit Score: 34.87  E-value: 2.02e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15242392    4 FIIDEDGKKYCVEVEKTTTIADMKTKIYDATG 35
Cdd:PRK12765 135 LTIFSNGKEYTITVDKSTTYRDLADKINEASG 166
Ubl_Sacsin cd17049
ubiquitin-like (Ubl) domain found in Sacsin and similar proteins; Sacsin, also termed DnaJ ...
 15-70 2.15e-03

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: 33.06  E-value: 2.15e-03
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242392 15 VEVEKTTTIADMKTKIYDATGMENAYQYLEHRGKivlEVHGGTTM-DDYKIKACDIF 70
Cdd:cd17049 17 FEVPPSAAVRDIKELIYEETDFPVSEQQLWHNGK---ELSDWVKIgGLVPSGSHEIF 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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