Protein : Qrob_P0020390.2 Q. robur
Protein Identifier  ? Qrob_P0020390.2 Organism . Name  Quercus robur
Score  28.1 Score Type  egn
Protein Description  (M=1) PTHR18929:SF84 - 5'-ADENYLYLSULFATE REDUCTASE-LIKE 5-RELATED (PTHR18929:SF84) Gene Prediction Quality  validated
Protein length 

Sequence

Length: 332  
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0 Synonyms

1 GO Terms

Identifier Name Description
GO:0045454 cell redox homeostasis Any process that maintains the redox environment of a cell or compartment within a cell.

40 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|mdm:103436245 10 328 + 319 Gaps:17 99.04 313 74.52 3e-165 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|mdm:103446576 10 328 + 319 Gaps:17 99.04 313 74.19 2e-164 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|mdm:103406080 10 328 + 319 Gaps:17 99.04 313 74.19 4e-164 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|pxb:103961869 10 328 + 319 Gaps:17 99.04 313 73.55 5e-163 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|pxb:103927161 10 328 + 319 Gaps:17 99.04 313 73.55 1e-162 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|pxb:103927176 10 328 + 319 Gaps:17 99.04 313 72.90 5e-162 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|fve:101312932 10 326 + 317 Gaps:17 97.47 316 73.38 6e-162 5'-adenylylsulfate reductase-like 4-like
blastp_kegg lcl|pmum:103319656 10 328 + 319 Gaps:17 99.04 313 72.58 1e-161 5'-adenylylsulfate reductase-like 4
blastp_kegg lcl|pop:POPTR_0002s09780g 13 331 + 319 Gaps:10 93.71 334 71.88 2e-156 POPTRDRAFT_551583 thioredoxin-related family protein
blastp_kegg lcl|cit:102628320 6 326 + 321 Gaps:19 96.88 320 72.58 5e-155 5'-adenylylsulfate reductase-like 4-like
blastp_pdb 2dj1_A 96 183 + 88 Gaps:3 65.00 140 35.16 1e-07 mol:protein length:140 Protein disulfide-isomerase A4
blastp_pdb 3idv_A 96 183 + 88 Gaps:7 37.76 241 35.16 5e-07 mol:protein length:241 Protein disulfide-isomerase A4
blastp_pdb 2diz_A 102 178 + 77 Gaps:4 69.23 117 35.80 3e-06 mol:protein length:117 Thioredoxin domain-containing protein 5
blastp_pdb 3uvt_E 102 178 + 77 Gaps:4 72.97 111 35.80 5e-06 mol:protein length:111 Thioredoxin domain-containing protein 5
blastp_pdb 3uvt_D 102 178 + 77 Gaps:4 72.97 111 35.80 5e-06 mol:protein length:111 Thioredoxin domain-containing protein 5
blastp_pdb 3uvt_C 102 178 + 77 Gaps:4 72.97 111 35.80 5e-06 mol:protein length:111 Thioredoxin domain-containing protein 5
blastp_pdb 3uvt_B 102 178 + 77 Gaps:4 72.97 111 35.80 5e-06 mol:protein length:111 Thioredoxin domain-containing protein 5
blastp_pdb 3uvt_A 102 178 + 77 Gaps:4 72.97 111 35.80 5e-06 mol:protein length:111 Thioredoxin domain-containing protein 5
blastp_uniprot_sprot sp|Q9SA00|APRL4_ARATH 45 321 + 277 Gaps:15 87.74 310 64.34 2e-115 5'-adenylylsulfate reductase-like 4 OS Arabidopsis thaliana GN APRL4 PE 2 SV 1
blastp_uniprot_sprot sp|Q84P95|APRL3_ORYSJ 34 324 + 291 Gaps:7 91.32 311 55.63 1e-97 5'-adenylylsulfate reductase-like 3 OS Oryza sativa subsp. japonica GN APRL3 PE 2 SV 1
blastp_uniprot_sprot sp|Q9ZPE9|APRL6_ARATH 45 316 + 272 Gaps:25 85.08 295 60.56 3e-89 5'-adenylylsulfate reductase-like 6 OS Arabidopsis thaliana GN APRL6 PE 2 SV 2
blastp_uniprot_sprot sp|Q67VZ8|APRL2_ORYSJ 46 325 + 280 Gaps:25 91.13 282 50.58 9e-72 5'-adenylylsulfate reductase-like 2 OS Oryza sativa subsp. japonica GN APRL2 PE 2 SV 1
blastp_uniprot_sprot sp|Q5DJV7|APRL4_ORYSJ 46 268 + 223 Gaps:3 84.85 264 49.55 2e-68 5'-adenylylsulfate reductase-like 4 OS Oryza sativa subsp. japonica GN APRL4 PE 2 SV 1
blastp_uniprot_sprot sp|Q93YX4|APRL5_ARATH 60 326 + 267 Gaps:27 85.33 300 37.89 1e-44 5'-adenylylsulfate reductase-like 5 OS Arabidopsis thaliana GN APRL5 PE 2 SV 1
blastp_uniprot_sprot sp|Q84JN1|APRL7_ARATH 60 324 + 265 Gaps:36 85.47 289 37.25 3e-40 5'-adenylylsulfate reductase-like 7 OS Arabidopsis thaliana GN APRL7 PE 2 SV 1
blastp_uniprot_sprot sp|Q84M47|APRL5_ORYSJ 57 311 + 255 Gaps:29 81.73 301 37.40 3e-36 5'-adenylylsulfate reductase-like 5 OS Oryza sativa subsp. japonica GN APRL5 PE 2 SV 1
blastp_uniprot_sprot sp|Q2QP53|APRL6_ORYSJ 95 326 + 232 Gaps:12 73.33 300 36.36 8e-32 5'-adenylylsulfate reductase-like 6 OS Oryza sativa subsp. japonica GN APRL6 PE 4 SV 1
blastp_uniprot_sprot sp|O13811|PDI2_SCHPO 102 198 + 97 Gaps:13 30.64 359 30.91 1e-06 Protein disulfide-isomerase C17H9.14c OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN SPAC17H9.14c PE 3 SV 1
rpsblast_cdd gnl|CDD|48548 80 179 + 100 none 100.00 100 60.00 9e-35 cd02999 PDI_a_ERp44_like PDIa family endoplasmic reticulum protein 44 (ERp44)-like subfamily composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif similar to ERp44. CXXS is still a redox active motif however the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER..
rpsblast_cdd gnl|CDD|48510 93 178 + 86 Gaps:6 89.11 101 31.11 2e-13 cd02961 PDI_a_family Protein Disulfide Isomerase (PDIa) family redox active TRX domains composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72 ERp57 (or ERp60) ERp44 P5 PDIR ERp46 and the transmembrane PDIs. PDI ERp57 ERp72 P5 PDIR and ERp46 are all oxidases catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1 which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29..

13 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 94 184 91 SSF52833 none none IPR012336
Phobius 20 27 8 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Pfam 92 178 87 PF00085 none Thioredoxin IPR013766
ProSiteProfiles 63 184 122 PS51352 none Thioredoxin domain profile. IPR012336
Phobius 257 331 75 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
PANTHER 94 253 160 PTHR18929 none none none
PANTHER 94 253 160 PTHR18929:SF84 none none none
Phobius 232 256 25 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 1 5 5 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Phobius 28 231 204 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 1 27 27 SIGNAL_PEPTIDE none Signal peptide region none
Gene3D 94 187 94 G3DSA:3.40.30.10 none none IPR012336
Phobius 6 19 14 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none

3 Localization

Analysis Start End Length
SignalP_EUK 1 27 26
SignalP_GRAM_POSITIVE 1 27 26
TMHMM 234 256 22

2 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2015_nEpis_3P Qrob_Chr12 12 s_1AOES6_1466 s_1B0DDG_1094 28,97 28,55 30,1 lod 3.6 8.4
Bourran2_2015_nP_3P Qrob_Chr12 12 v_10140_295 v_838_303 16 14,69 18,01 lod 5.1 13.7

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 27   Secretory pathway 1 0.900 0.068 NON-PLANT 27