Protein : Qrob_P0142010.2 Q. robur
Protein Identifier  ? Qrob_P0142010.2 Organism . Name  Quercus robur
Score  40.3 Score Type  egn
Protein Description  (M=1) PTHR13009//PTHR13009:SF0 - HEAT SHOCK PROTEIN 90 (HSP90) CO-CHAPERONE AHA-1 // SUBFAMILY NOT NAMED Gene Prediction Quality  validated
Protein length 

Sequence

Length: 363  
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0051087 chaperone binding Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
GO:0006950 response to stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
GO:0001671 ATPase activator activity Binds to and increases the ATP hydrolysis activity of an ATPase.

34 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_024944 1 362 + 362 Gaps:10 100.00 352 78.98 0.0 Aha1 domain-containing protein isoform 1
blastp_kegg lcl|pxb:103958793 1 362 + 362 Gaps:14 100.00 348 78.74 0.0 activator of 90 kDa heat shock protein ATPase homolog
blastp_kegg lcl|aly:ARALYDRAFT_478557 1 362 + 362 Gaps:2 100.00 360 73.33 0.0 Aha1 domain-containing protein
blastp_kegg lcl|rcu:RCOM_0278300 1 362 + 362 Gaps:10 100.00 352 79.55 0.0 Hsp90 co-chaperone AHA1 putative
blastp_kegg lcl|fve:101308889 1 362 + 362 Gaps:15 100.00 347 76.37 0.0 activator of 90 kDa heat shock protein ATPase homolog 1-like
blastp_kegg lcl|crb:CARUB_v10014031mg 1 362 + 362 Gaps:4 100.00 362 72.38 0.0 hypothetical protein
blastp_kegg lcl|cit:102621083 1 362 + 362 Gaps:5 100.00 357 74.79 0.0 activator of 90 kDa heat shock protein ATPase homolog
blastp_kegg lcl|pop:POPTR_0006s20890g 1 362 + 362 Gaps:16 100.00 346 79.48 0.0 POPTRDRAFT_561237 aha1 domain-containing family protein
blastp_kegg lcl|ath:AT3G12050 1 362 + 362 Gaps:2 100.00 360 72.78 0.0 Aha1 domain-containing protein
blastp_kegg lcl|cic:CICLE_v10012043mg 1 362 + 362 Gaps:6 100.00 360 75.56 0.0 hypothetical protein
blastp_pdb 1x53_A 228 361 + 134 Gaps:12 86.90 145 36.51 4e-16 mol:protein length:145 Activator of 90 kDa heat shock protein ATPase
blastp_pdb 3ni8_A 230 360 + 131 Gaps:1 83.54 158 29.55 2e-14 mol:protein length:158 PFC0360w protein
blastp_pdb 1usv_H 21 133 + 113 Gaps:1 65.88 170 30.36 5e-13 mol:protein length:170 AHA1
blastp_pdb 1usv_F 21 133 + 113 Gaps:1 65.88 170 30.36 5e-13 mol:protein length:170 AHA1
blastp_pdb 1usv_D 21 133 + 113 Gaps:1 65.88 170 30.36 5e-13 mol:protein length:170 AHA1
blastp_pdb 1usv_B 21 133 + 113 Gaps:1 65.88 170 30.36 5e-13 mol:protein length:170 AHA1
blastp_pdb 1usu_B 21 133 + 113 Gaps:1 65.88 170 29.46 1e-12 mol:protein length:170 AHA1
blastp_uniprot_sprot sp|Q8BK64|AHSA1_MOUSE 1 361 + 361 Gaps:31 98.82 338 36.53 2e-48 Activator of 90 kDa heat shock protein ATPase homolog 1 OS Mus musculus GN Ahsa1 PE 2 SV 2
blastp_uniprot_sprot sp|O95433|AHSA1_HUMAN 1 361 + 361 Gaps:39 98.82 338 36.23 4e-48 Activator of 90 kDa heat shock protein ATPase homolog 1 OS Homo sapiens GN AHSA1 PE 1 SV 1
blastp_uniprot_sprot sp|Q8N9S3|AHSA2_MOUSE 1 358 + 358 Gaps:34 97.89 331 35.19 6e-42 Activator of 90 kDa heat shock protein ATPase homolog 2 OS Mus musculus GN Ahsa2 PE 2 SV 2
blastp_uniprot_sprot sp|Q55DB6|AHSA_DICDI 1 360 + 360 Gaps:54 98.69 383 29.10 1e-39 Activator of 90 kDa heat shock protein ATPase homolog OS Dictyostelium discoideum GN ahsa PE 2 SV 1
blastp_uniprot_sprot sp|A6QQC0|AHSA2_BOVIN 1 272 + 272 Gaps:39 95.77 260 37.75 4e-30 Activator of 90 kDa heat shock protein ATPase homolog 2 OS Bos taurus GN AHSA2 PE 2 SV 1
blastp_uniprot_sprot sp|Q9P782|YNY8_SCHPO 21 361 + 341 Gaps:54 97.32 336 28.75 8e-29 Uncharacterized protein C1711.08 OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN SPBC1711.08 PE 2 SV 1
blastp_uniprot_sprot sp|Q12449|AHA1_YEAST 21 361 + 341 Gaps:42 98.00 350 27.11 2e-23 Hsp90 co-chaperone AHA1 OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN AHA1 PE 1 SV 1
blastp_uniprot_sprot sp|Q719I0|AHSA2_HUMAN 1 322 + 322 Gaps:74 88.29 299 36.74 1e-22 Activator of 90 kDa heat shock protein ATPase homolog 2 OS Homo sapiens GN AHSA2 PE 2 SV 2
blastp_uniprot_sprot sp|P53834|HCH1_YEAST 21 119 + 99 Gaps:5 67.97 153 26.92 2e-07 Hsp90 co-chaperone HCH1 OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN HCH1 PE 1 SV 1
rpsblast_cdd gnl|CDD|176901 227 360 + 134 Gaps:8 100.00 126 48.41 4e-42 cd08892 SRPBCC_Aha1 Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins. This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1 and related domains. Proteins in this group belong to the SRPBCC domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Aha1 is one of several co-chaperones which regulate the dimeric chaperone Hsp90. Hsp90 Aha1 and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90 and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation depending on the client protein for example it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. The mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.
rpsblast_cdd gnl|CDD|204172 29 165 + 137 Gaps:4 97.08 137 33.83 8e-27 pfam09229 Aha1_N Activator of Hsp90 ATPase N-terminal. Members of this family which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet followed by a C-terminal alpha-helix. The two helices are packed together with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.
rpsblast_cdd gnl|CDD|198068 29 163 + 135 Gaps:4 97.76 134 29.01 4e-24 smart01000 Aha1_N Activator of Hsp90 ATPase N-terminal. This domain is predominantly found in the protein 'Activator of Hsp90 ATPase' it adopts a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet followed by a C-terminal alpha-helix. The two helices are packed together with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.
rpsblast_cdd gnl|CDD|35139 21 361 + 341 Gaps:80 97.43 272 29.43 1e-18 COG5580 COG5580 Activator of HSP90 ATPase [Posttranslational modification protein turnover chaperones].

8 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 239 358 120 PF08327 none Activator of Hsp90 ATPase homolog 1-like protein IPR013538
SMART 29 165 137 SM01000 none Activator of Hsp90 ATPase, N-terminal IPR015310
PANTHER 2 362 361 PTHR13009 none none none
SUPERFAMILY 227 361 135 SSF55961 none none none
Gene3D 212 357 146 G3DSA:3.30.530.20 none none IPR023393
SUPERFAMILY 21 165 145 SSF103111 none none IPR015310
PANTHER 2 362 361 PTHR13009:SF0 none none none
Pfam 29 164 136 PF09229 none Activator of Hsp90 ATPase, N-terminal IPR015310

0 Localization

9 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_nPriLBD_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,36 0 30,43 lod 2,5806 5,1
Bourran2_2014_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2015_nSeqBC_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,06 25,47 27,72 lod 3.6 7.1
Bourran2_2014_nP_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 7,9 0,09 30,09 lod 2,3636 5
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran2_2015_nEpiBC_A4 Qrob_Chr07 7 s_1DP9TW_798 v_8128_173 22,61 22,14 22,73 lod 3.1 8.5
Bourran2_2014_nEpiBC_A4 Qrob_Chr07 7 s_2FI9D9_500 s_1AXDMJ_325 12,26 0 34,9 lod 2,2306 6,1
Bourran2_2014_nPriBD_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 5,54 0,4 20,6 lod 2,6345 5,9

0 Targeting