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Conserved domains on  [gi|186510943|ref|NP_190746|]
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BCL-2-associated athanogene 4 [Arabidopsis thaliana]

Protein Classification

BAG family molecular chaperone regulator; ubiquitin family protein( domain architecture ID 13018406)

BAG family molecular chaperone regulator which may function as a co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses; similar to Arabidopsis thaliana BAG family molecular chaperone regulator 3 which binds to the ATPase domain of HSP70/HSC70 chaperones; contains a BAG domain and a ubiquitin-like domain| ubiquitin family protein belongs to a diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes; has an N-terminal domain with similarity to the N-terminus of ubiquitin fusion degradation UFD1 which functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl_AtBAG1_like cd17054
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, ...
47-116 3.47e-32

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, AtBAG2, AtBAG3, AtBAG4, and similar proteins; The family includes four Arabidopsis BAG family proteins (AtBAG1, AtBAG2, AtBAG3, AtBAG4) that have very similar domain organizations with a ubiquitin-like (Ubl) domain in the N-terminus and a BAG domain in the C-terminus. They may function as co-chaperones that regulate diverse cellular pathways, such as programmed cell death and stress responses. AtBAG1, AtBAG3, and AtBAG4 are predicted to localize in the cytoplasm, but the localization of AtBAG2 is the microbody. AtBAG4 can interact with Hsc70. The overexpression of AtBAG4 in tobacco plants confers tolerance to a wide range of abiotic stresses such as UV light, cold, oxidants, and salt treatments.


:

Pssm-ID: 340574  Cd Length: 70  Bit Score: 113.28  E-value: 3.47e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510943  47 TIRITVSHGSSHHDLHISAHATFGDVKKALVQKTGLEASELKILFRGVERDDAEQLQAAGVKDASKLVVV 116
Cdd:cd17054    1 TIKIKVSHGAVYHEVTVSAQATFGDLKKLLVQDTGLQPQEQKLLFRGKEKDDKDFLDLAGVKDKAKVVLV 70
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
142-218 4.89e-16

BAG domain; Domain present in Hsp70 regulators.


:

Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 71.11  E-value: 4.89e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186510943  142 VNAVTGEVDKLSDRVVALEVAVNggTQVAVREFDMAAELLMRQLLKLDGIEAEGD--AKVQRKAEVRRIQNLQEAVDKL 218
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEGSPP--SKKRDKEYKRLSEMLMKLLLKLDGIDTEGDpeAREARKAAVKEVQGLLEKLDAL 77
 
Name Accession Description Interval E-value
Ubl_AtBAG1_like cd17054
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, ...
47-116 3.47e-32

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, AtBAG2, AtBAG3, AtBAG4, and similar proteins; The family includes four Arabidopsis BAG family proteins (AtBAG1, AtBAG2, AtBAG3, AtBAG4) that have very similar domain organizations with a ubiquitin-like (Ubl) domain in the N-terminus and a BAG domain in the C-terminus. They may function as co-chaperones that regulate diverse cellular pathways, such as programmed cell death and stress responses. AtBAG1, AtBAG3, and AtBAG4 are predicted to localize in the cytoplasm, but the localization of AtBAG2 is the microbody. AtBAG4 can interact with Hsc70. The overexpression of AtBAG4 in tobacco plants confers tolerance to a wide range of abiotic stresses such as UV light, cold, oxidants, and salt treatments.


Pssm-ID: 340574  Cd Length: 70  Bit Score: 113.28  E-value: 3.47e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510943  47 TIRITVSHGSSHHDLHISAHATFGDVKKALVQKTGLEASELKILFRGVERDDAEQLQAAGVKDASKLVVV 116
Cdd:cd17054    1 TIKIKVSHGAVYHEVTVSAQATFGDLKKLLVQDTGLQPQEQKLLFRGKEKDDKDFLDLAGVKDKAKVVLV 70
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
142-218 4.89e-16

BAG domain; Domain present in Hsp70 regulators.


Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 71.11  E-value: 4.89e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186510943  142 VNAVTGEVDKLSDRVVALEVAVNggTQVAVREFDMAAELLMRQLLKLDGIEAEGD--AKVQRKAEVRRIQNLQEAVDKL 218
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEGSPP--SKKRDKEYKRLSEMLMKLLLKLDGIDTEGDpeAREARKAAVKEVQGLLEKLDAL 77
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
138-219 9.07e-14

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


Pssm-ID: 214591  Cd Length: 79  Bit Score: 65.02  E-value: 9.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510943   138 AIAAVNAVTGEVDKlsdrVVALEVAVNGGtQVAVREFDMAAELLMRQLLKLDGIEAEG--DAKVQRKAEVRRIQNLQEAV 215
Cdd:smart00264   1 SIKKINEVLDEVQK----KIEKEVQVADG-KKDDKEYLRLSEELMKLLLKLDSVDVEGceDIREARKRLVRLIQNLLNAL 75

                   ....
gi 186510943   216 DKLK 219
Cdd:smart00264  76 DSKK 79
 
Name Accession Description Interval E-value
Ubl_AtBAG1_like cd17054
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, ...
47-116 3.47e-32

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, AtBAG2, AtBAG3, AtBAG4, and similar proteins; The family includes four Arabidopsis BAG family proteins (AtBAG1, AtBAG2, AtBAG3, AtBAG4) that have very similar domain organizations with a ubiquitin-like (Ubl) domain in the N-terminus and a BAG domain in the C-terminus. They may function as co-chaperones that regulate diverse cellular pathways, such as programmed cell death and stress responses. AtBAG1, AtBAG3, and AtBAG4 are predicted to localize in the cytoplasm, but the localization of AtBAG2 is the microbody. AtBAG4 can interact with Hsc70. The overexpression of AtBAG4 in tobacco plants confers tolerance to a wide range of abiotic stresses such as UV light, cold, oxidants, and salt treatments.


Pssm-ID: 340574  Cd Length: 70  Bit Score: 113.28  E-value: 3.47e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510943  47 TIRITVSHGSSHHDLHISAHATFGDVKKALVQKTGLEASELKILFRGVERDDAEQLQAAGVKDASKLVVV 116
Cdd:cd17054    1 TIKIKVSHGAVYHEVTVSAQATFGDLKKLLVQDTGLQPQEQKLLFRGKEKDDKDFLDLAGVKDKAKVVLV 70
BAG pfam02179
BAG domain; Domain present in Hsp70 regulators.
142-218 4.89e-16

BAG domain; Domain present in Hsp70 regulators.


Pssm-ID: 460475 [Multi-domain]  Cd Length: 77  Bit Score: 71.11  E-value: 4.89e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186510943  142 VNAVTGEVDKLSDRVVALEVAVNggTQVAVREFDMAAELLMRQLLKLDGIEAEGD--AKVQRKAEVRRIQNLQEAVDKL 218
Cdd:pfam02179   1 IDAILKEVDKLEPQVEAFEGSPP--SKKRDKEYKRLSEMLMKLLLKLDGIDTEGDpeAREARKAAVKEVQGLLEKLDAL 77
BAG smart00264
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ...
138-219 9.07e-14

BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains


Pssm-ID: 214591  Cd Length: 79  Bit Score: 65.02  E-value: 9.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510943   138 AIAAVNAVTGEVDKlsdrVVALEVAVNGGtQVAVREFDMAAELLMRQLLKLDGIEAEG--DAKVQRKAEVRRIQNLQEAV 215
Cdd:smart00264   1 SIKKINEVLDEVQK----KIEKEVQVADG-KKDDKEYLRLSEELMKLLLKLDSVDVEGceDIREARKRLVRLIQNLLNAL 75

                   ....
gi 186510943   216 DKLK 219
Cdd:smart00264  76 DSKK 79
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
50-116 1.09e-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: 47.98  E-value: 1.09e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186510943  50 ITVSHGSSH-HDLHISAHATFGDVKKALVQKTGLEASELKILFRGVERDDAEQLQAAGVKDASKLVVV 116
Cdd:cd17039    1 ITVKTLDGKtYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
49-116 2.31e-07

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 47.27  E-value: 2.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186510943  49 RITVSHGSSHHDLHISA----HATFGDVKKALVQKTGLEASELKILFRG-VERDDAEQLQAAGVKDASKLVVV 116
Cdd:cd01812    2 TVTVIHGSNKHTIELPSqdedEPTLQDLAEAIEEVTGVPVENQKLIFKGkSLKDPEQPLSALGVKNGSKIMLI 74
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
48-116 5.22e-04

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 37.61  E-value: 5.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186510943  48 IRITVSHGSSHHDLHISAHATFGDVKKALVQKTGLEASELKILFRGVERDDAeQLQAAGVKDASKLVVV 116
Cdd:cd17047    1 VDFKVIWNKEKYDVKFPLDSTIAELKEHIETLTGVPPAMQKLMYKGLLKDDK-TLRELKVTKGAKVMVV 68
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
48-109 2.45e-03

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: 35.69  E-value: 2.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186510943  48 IRITV-SHGSSHHDLHISAHATFGDVKKALVQKTGLEASELKILFRGVERDDAEQLQAAGVKD 109
Cdd:cd16106    1 IKVTVkCSNGKKFTVEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSYKIQD 63
 
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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