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Conserved domains on  [gi|552819621|ref|XP_005845453|]
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hypothetical protein CHLNCDRAFT_137085 [Chlorella variabilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HYPK_UBA pfam19026
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ...
 72-112 5.03e-14

HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK protein and its homologs. This domain in HYPK mediates a protein interaction with the Naa15 C-terminus.


:

Pssm-ID: 436907  Cd Length: 41  Bit Score: 66.04  E-value: 5.03e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 552819621   72 VKVQKEDIEVIAQQFDMDKKKAERALRENGGELKTALQSLL 112
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 302-351 4.36e-06

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.


:

Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 43.69  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 552819621 302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKC-GAAGASDAMSIVADCYAML 351
Cdd:cd06257    4 DILGVPPDA-SDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVL 53
TIGR00264 super family cl29458
alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its ...
 28-111 5.01e-05

alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its C-terminal domain of about 40 amino acids is homologous to the C-termini of the nascent polypeptide-associated complex alpha chain (alpha-NAC) and its yeast ortholog Egd2p and to the huntingtin-interacting protein HYPK. It shows weaker similarity, possibly through shared structural constraints rather than through homology, with the amino-terminal domain of elongation factor Ts. Alpha-NAC plays a role in preventing nascent polypeptides from binding inappropriately to membrane-targeting apparatus during translation, but is also active as a transcription regulator. [Unknown function, General]


The actual alignment was detected with superfamily member TIGR00264:

Pssm-ID: 272988 [Multi-domain]  Cd Length: 116  Bit Score: 42.63  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552819621   28 DFREEKEMMTNVDKELV-----QQAMQKLAAEQAQRTEAQRQRERElAAVKVQKEDIEVIAQQFDMDKKKAERALRENGG 102
Cdd:TIGR00264  27 DLDVEEVIIVFDDEEWIfenpkVQVMDILGVKTYQITGKPKKEKVE-EEEEITEDDIELVMKQCNVSKEEARRALEECGG 105


                  ....*....
gi 552819621  103 ELKTALQSL 111
Cdd:TIGR00264 106 DLAEAIMKL 114
 
Name Accession Description Interval E-value
HYPK_UBA pfam19026
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ...
 72-112 5.03e-14

HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK protein and its homologs. This domain in HYPK mediates a protein interaction with the Naa15 C-terminus.


Pssm-ID: 436907  Cd Length: 41  Bit Score: 66.04  E-value: 5.03e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 552819621   72 VKVQKEDIEVIAQQFDMDKKKAERALRENGGELKTALQSLL 112
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41
UBA_HYPK cd14361
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ...
 72-112 8.94e-13

UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K, is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It is involved in regulating cell growth, cell cycle, unfolded protein response, and cell death. All members in this subfamily contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes.


Pssm-ID: 270544  Cd Length: 41  Bit Score: 62.14  E-value: 8.94e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 552819621  72 VKVQKEDIEVIAQQFDMDKKKAERALRENGGELKTALQSLL 112
Cdd:cd14361    1 VKVKKEDVELIVNELEVSKAQAERALREHNGDVVKALRALI 41
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 302-351 4.36e-06

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.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 43.69  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 552819621 302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKC-GAAGASDAMSIVADCYAML 351
Cdd:cd06257    4 DILGVPPDA-SDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVL 53
DnaJ smart00271
DnaJ molecular chaperone homology domain;
302-351 2.34e-05

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 41.84  E-value: 2.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 552819621   302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKCG--AAGASDAMSIVADCYAML 351
Cdd:smart00271   5 EILGVPRDA-SLDEIKKAYRKLALKYHPDKNPgdKEEAEEKFKEINEAYEVL 55
TIGR00264 TIGR00264
alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its ...
 28-111 5.01e-05

alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its C-terminal domain of about 40 amino acids is homologous to the C-termini of the nascent polypeptide-associated complex alpha chain (alpha-NAC) and its yeast ortholog Egd2p and to the huntingtin-interacting protein HYPK. It shows weaker similarity, possibly through shared structural constraints rather than through homology, with the amino-terminal domain of elongation factor Ts. Alpha-NAC plays a role in preventing nascent polypeptides from binding inappropriately to membrane-targeting apparatus during translation, but is also active as a transcription regulator. [Unknown function, General]


Pssm-ID: 272988 [Multi-domain]  Cd Length: 116  Bit Score: 42.63  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552819621   28 DFREEKEMMTNVDKELV-----QQAMQKLAAEQAQRTEAQRQRERElAAVKVQKEDIEVIAQQFDMDKKKAERALRENGG 102
Cdd:TIGR00264  27 DLDVEEVIIVFDDEEWIfenpkVQVMDILGVKTYQITGKPKKEKVE-EEEEITEDDIELVMKQCNVSKEEARRALEECGG 105


                  ....*....
gi 552819621  103 ELKTALQSL 111
Cdd:TIGR00264 106 DLAEAIMKL 114
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 302-351 1.41e-04

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: 39.76  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 552819621  302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKC-GAAGASDAMSIVADCYAML 351
Cdd:pfam00226   4 EILGVSPDA-SDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVL 53
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
302-341 1.12e-03

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.47  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 552819621 302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKCgAAGASDAM 341
Cdd:COG1076    8 ELLGLPPDA-DDAELKRAYRKLQREHHPDRL-AAGLPEEE 45
 
Name Accession Description Interval E-value
HYPK_UBA pfam19026
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ...
 72-112 5.03e-14

HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK protein and its homologs. This domain in HYPK mediates a protein interaction with the Naa15 C-terminus.


Pssm-ID: 436907  Cd Length: 41  Bit Score: 66.04  E-value: 5.03e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 552819621   72 VKVQKEDIEVIAQQFDMDKKKAERALRENGGELKTALQSLL 112
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41
UBA_HYPK cd14361
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ...
 72-112 8.94e-13

UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K, is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It is involved in regulating cell growth, cell cycle, unfolded protein response, and cell death. All members in this subfamily contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes.


Pssm-ID: 270544  Cd Length: 41  Bit Score: 62.14  E-value: 8.94e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 552819621  72 VKVQKEDIEVIAQQFDMDKKKAERALRENGGELKTALQSLL 112
Cdd:cd14361    1 VKVKKEDVELIVNELEVSKAQAERALREHNGDVVKALRALI 41
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 302-351 4.36e-06

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.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 43.69  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 552819621 302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKC-GAAGASDAMSIVADCYAML 351
Cdd:cd06257    4 DILGVPPDA-SDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVL 53
DnaJ smart00271
DnaJ molecular chaperone homology domain;
302-351 2.34e-05

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 41.84  E-value: 2.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 552819621   302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKCG--AAGASDAMSIVADCYAML 351
Cdd:smart00271   5 EILGVPRDA-SLDEIKKAYRKLALKYHPDKNPgdKEEAEEKFKEINEAYEVL 55
TIGR00264 TIGR00264
alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its ...
 28-111 5.01e-05

alpha-NAC-related protein; This hypothetical protein is found so far only in the Archaea. Its C-terminal domain of about 40 amino acids is homologous to the C-termini of the nascent polypeptide-associated complex alpha chain (alpha-NAC) and its yeast ortholog Egd2p and to the huntingtin-interacting protein HYPK. It shows weaker similarity, possibly through shared structural constraints rather than through homology, with the amino-terminal domain of elongation factor Ts. Alpha-NAC plays a role in preventing nascent polypeptides from binding inappropriately to membrane-targeting apparatus during translation, but is also active as a transcription regulator. [Unknown function, General]


Pssm-ID: 272988 [Multi-domain]  Cd Length: 116  Bit Score: 42.63  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552819621   28 DFREEKEMMTNVDKELV-----QQAMQKLAAEQAQRTEAQRQRERElAAVKVQKEDIEVIAQQFDMDKKKAERALRENGG 102
Cdd:TIGR00264  27 DLDVEEVIIVFDDEEWIfenpkVQVMDILGVKTYQITGKPKKEKVE-EEEEITEDDIELVMKQCNVSKEEARRALEECGG 105


                  ....*....
gi 552819621  103 ELKTALQSL 111
Cdd:TIGR00264 106 DLAEAIMKL 114
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 302-351 1.41e-04

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: 39.76  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 552819621  302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKC-GAAGASDAMSIVADCYAML 351
Cdd:pfam00226   4 EILGVSPDA-SDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVL 53
UBA_NAC_like cd14278
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and ...
 76-111 2.91e-04

UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins; The family contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins found in archaea and bacteria. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. The family also includes huntingtin-interacting protein K (HYPK), also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K. It is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It may be involved in regulating cell growth, cell cycle, unfolded protein response and cell death. All members in this family contain an ubiquitin-associated (UBA) domain.


Pssm-ID: 270464 [Multi-domain]  Cd Length: 37  Bit Score: 38.23  E-value: 2.91e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 552819621  76 KEDIEVIAQQFDMDKKKAERALRENGGELKTALQSL 111
Cdd:cd14278    1 EEDIELVMSQTGVSREEAIKALRENKGDVVDAILEL 36
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
302-341 1.12e-03

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.47  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 552819621 302 EVLRVPRKCgDPSALRAAYRRVSMAVHPDKCgAAGASDAM 341
Cdd:COG1076    8 ELLGLPPDA-DDAELKRAYRKLQREHHPDRL-AAGLPEEE 45
UBA_AeNAC cd14359
UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from ...
 73-111 2.82e-03

UBA-like domain found in archaeal nascent polypeptide-associated complex homolog from Methanothermobacter marburgensis (AeNAC) and similar proteins; AeNAC is a functional archaeal homolog of eukaryotic nascent polypeptide-associated complex (NAC). Both AeNAC and eukaryotic NAC function as the cytosolic chaperone that can bind to ribosomal RNA, interact with the nascent polypeptide chains as they emerge from the ribosome, and assist in post-translational processes. They all contain a NAC domain and an ubiquitin-associated (UBA) domain in the C-terminus. However, unlike eukaryotic NAC, AeNAC forms a ribosome associated homodimer, but not heterodimer. The NAC domain of AeNAC is responsible for the homodimer formation.


Pssm-ID: 270542 [Multi-domain]  Cd Length: 40  Bit Score: 35.28  E-value: 2.82e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 552819621  73 KVQKEDIEVIAQQFDMDKKKAERALRENGGELKTALQSL 111
Cdd:cd14359    1 EISEEDIELVMEQTGVSREEARKALEESGGDLAEAILKL 39
 
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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