Protein : Qrob_P0087780.2 Q. robur
Protein Identifier  ? Qrob_P0087780.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=52) 5.2.1.8 - Peptidylprolyl isomerase. Code Enzyme  EC:5.2.1.8
Gene Prediction Quality  validated Protein length 

Sequence

Length: 341  
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0006457 protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
GO:0000413 protein peptidyl-prolyl isomerization The modification of a protein by cis-trans isomerization of a proline residue.
GO:0003755 peptidyl-prolyl cis-trans isomerase activity Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).

13 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100853434 1 338 + 338 Gaps:11 97.68 345 76.26 0.0 uncharacterized LOC100853434
blastp_kegg lcl|pper:PRUPE_ppa006955mg 1 339 + 339 Gaps:2 87.66 389 73.61 0.0 hypothetical protein
blastp_kegg lcl|vvi:100854739 1 338 + 338 Gaps:11 97.68 345 75.37 0.0 uncharacterized LOC100854739
blastp_kegg lcl|pop:POPTR_0003s08220g 1 340 + 340 Gaps:5 100.00 335 74.63 0.0 hypothetical protein
blastp_kegg lcl|pxb:103937905 1 339 + 339 Gaps:3 98.56 347 76.32 0.0 uncharacterized LOC103937905
blastp_kegg lcl|fve:101307592 1 338 + 338 Gaps:2 98.82 340 73.21 0.0 uncharacterized protein LOC101307592
blastp_kegg lcl|pmum:103342610 1 339 + 339 Gaps:2 98.55 346 72.73 0.0 uncharacterized LOC103342610
blastp_kegg lcl|pop:POPTR_0003s03180g 1 330 + 330 Gaps:5 96.15 338 76.00 0.0 hypothetical protein
blastp_kegg lcl|cit:102623933 3 334 + 332 Gaps:4 95.91 342 73.48 4e-179 hypothetical protein
blastp_kegg lcl|tcc:TCM_015838 1 338 + 338 Gaps:1 98.25 343 74.48 2e-178 Peptidyl-prolyl cis-trans isomerases isoform 1
rpsblast_cdd gnl|CDD|201045 168 310 + 143 Gaps:30 90.97 144 34.35 6e-13 pfam00160 Pro_isomerase Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD. The peptidyl-prolyl cis-trans isomerases also known as cyclophilins share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyze peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.
rpsblast_cdd gnl|CDD|29390 168 320 + 153 Gaps:34 99.32 146 28.97 1e-08 cd00317 cyclophilin cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40 a co-chaperone of the hsp90 chaperone system human cyclophilin A a chaperone in the HIV-1 infectious process and human cyclophilin H a component of the U4/U6 snRNP whose isomerization or chaperoning activities may play a role in RNA splicing. .
rpsblast_cdd gnl|CDD|30997 165 307 + 143 Gaps:11 86.08 158 31.62 3e-08 COG0652 PpiB Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification protein turnover chaperones].

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 1 15 15 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 38 340 303 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
SUPERFAMILY 161 319 159 SSF50891 none none IPR029000
Pfam 167 308 142 PF00160 none Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD IPR002130
ProSiteProfiles 1 26 26 PS51257 none Prokaryotic membrane lipoprotein lipid attachment site profile. none
Gene3D 163 309 147 G3DSA:2.40.100.10 none none IPR029000
Phobius 16 37 22 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none

1 Localization

Analysis Start End Length
TMHMM 15 37 22

7 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_vSeqBC_3P Qrob_Chr10 10 s_1A6CK6_610 v_7092_29 4,28 0 23,27 lod 2,8619 7
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_2014_nFork*_3P Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,28 7,43 41,48 lod 2,4044 5,5
Bourran1_2004_QTL4_peak_Bud_burst_3P Qrob_Chr04 4 s_1AHUWN_1101 s_1BRNG7_1618 30,55 0 47,55 lod 2,8 7,4
Bourran2_2002_QTL10_peak_Bud_burst_A4 Qrob_Chr04 4 s_1B59MJ_737 s_1BGLSD_999 15,86 0 41,66 lod 2,8 4
Bourran1_2000_QTL3_peak_Bud_burst_3P Qrob_Chr04 4 s_1A6DJQ_418 s_1A1PEC_1268 23,09 9,09 44,09 lod 2,3 6,8
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL7_d13Cf Qrob_Chr04 4 s_1B91MJ_705 s_1AHIKX_640 33.92 12,11 48,31 lod 6.1865 0.023

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 31   Secretory pathway 1 0.949 0.026 NON-PLANT 31