Protein : Qrob_P0246330.2 Q. robur
Protein Identifier  ? Qrob_P0246330.2 Organism . Name  Quercus robur
Score  97.0 Score Type  egn
Protein Description  (M=2) PTHR11071:SF17 - PEPTIDYL-PROLYL CIS-TRANS ISOMERASE Code Enzyme  EC:5.2.1.8
Gene Prediction Quality  validated Protein length 

Sequence

Length: 111  
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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).

26 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0010s01660g 5 84 + 80 Gaps:18 43.95 223 67.35 7e-36 POPTRDRAFT_657869 peptidyl-prolyl cis-trans isomerase cyclophilin-type family protein
blastp_kegg lcl|pper:PRUPE_ppa013253mg 5 84 + 80 Gaps:18 74.24 132 64.29 2e-35 hypothetical protein
blastp_kegg lcl|pmum:103321603 6 84 + 79 Gaps:18 40.25 241 65.98 2e-34 peptidyl-prolyl cis-trans isomerase-like 3
blastp_kegg lcl|vvi:100244863 5 84 + 80 Gaps:18 43.36 226 65.31 7e-34 probable peptidyl-prolyl cis-trans isomerase-like
blastp_kegg lcl|fve:101309243 5 84 + 80 Gaps:18 42.42 231 64.29 2e-33 probable peptidyl-prolyl cis-trans isomerase-like
blastp_kegg lcl|tcc:TCM_011738 5 84 + 80 Gaps:18 36.70 267 64.29 8e-33 Cyclophilin-like peptidyl-prolyl cis-trans isomerase family protein isoform 1
blastp_kegg lcl|cmo:103485795 2 84 + 83 Gaps:18 43.16 234 60.40 2e-32 peptidyl-prolyl cis-trans isomerase-like 3
blastp_kegg lcl|mdm:103402911 6 84 + 79 Gaps:18 40.25 241 61.86 3e-32 peptidyl-prolyl cis-trans isomerase-like 3
blastp_kegg lcl|pxb:103950844 5 84 + 80 Gaps:18 42.24 232 62.24 3e-32 peptidyl-prolyl cis-trans isomerase CYP23
blastp_kegg lcl|eus:EUTSA_v10008695mg 5 83 + 79 Gaps:18 42.92 226 62.89 4e-32 hypothetical protein
blastp_pdb 2ok3_A 8 53 + 46 none 28.57 161 43.48 5e-07 mol:protein length:161 Peptidyl-prolyl cis-trans isomerase-like 3
blastp_pdb 1xyh_A 8 53 + 46 none 28.57 161 43.48 5e-07 mol:protein length:161 cyclophilin-like protein PPIL3b
blastp_pdb 2oju_B 8 53 + 46 none 27.54 167 43.48 6e-07 mol:protein length:167 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 3
blastp_pdb 2oju_A 8 53 + 46 none 27.54 167 43.48 6e-07 mol:protein length:167 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 3
blastp_uniprot_sprot sp|P0CP84|PPIL1_CRYNJ 8 78 + 71 none 40.80 174 29.58 9e-07 Peptidyl-prolyl cis-trans isomerase-like 1 OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) GN CYP1 PE 3 SV 1
blastp_uniprot_sprot sp|P0CP85|PPIL1_CRYNB 8 78 + 71 none 40.80 174 29.58 9e-07 Peptidyl-prolyl cis-trans isomerase-like 1 OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) GN CYP1 PE 3 SV 1
blastp_uniprot_sprot sp|Q5ZLV2|PPIL3_CHICK 8 53 + 46 none 28.57 161 43.48 2e-06 Peptidyl-prolyl cis-trans isomerase-like 3 OS Gallus gallus GN PPIL3 PE 2 SV 1
blastp_uniprot_sprot sp|Q9D6L8|PPIL3_MOUSE 8 53 + 46 none 28.57 161 43.48 2e-06 Peptidyl-prolyl cis-trans isomerase-like 3 OS Mus musculus GN Ppil3 PE 2 SV 1
blastp_uniprot_sprot sp|Q9H2H8|PPIL3_HUMAN 8 53 + 46 none 28.57 161 43.48 2e-06 Peptidyl-prolyl cis-trans isomerase-like 3 OS Homo sapiens GN PPIL3 PE 1 SV 1
blastp_uniprot_sprot sp|Q812D3|PPIL3_RAT 8 53 + 46 none 28.57 161 43.48 2e-06 Peptidyl-prolyl cis-trans isomerase-like 3 OS Rattus norvegicus GN Ppil3 PE 2 SV 1
blastp_uniprot_sprot sp|Q7SF72|PPIL1_NEUCR 8 54 + 47 none 28.83 163 40.43 8e-06 Peptidyl-prolyl cis-trans isomerase-like 1 OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) GN ppi-1 PE 3 SV 2
rpsblast_cdd gnl|CDD|201045 8 56 + 49 none 34.03 144 48.98 2e-10 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 6 59 + 54 none 36.99 146 29.63 2e-09 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 6 73 + 68 none 43.04 158 29.41 2e-09 COG0652 PpiB Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification protein turnover chaperones].
rpsblast_cdd gnl|CDD|29394 8 67 + 60 none 37.74 159 35.00 5e-07 cd01923 cyclophilin_RING cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins Human hCyP-60 and Caenorhabditis elegans MOG-6 which compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and C. elegans MOG-6 to physically interact with MEP-1 a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination..
rpsblast_kog gnl|CDD|36101 8 67 + 60 none 11.58 518 33.33 8e-08 KOG0883 KOG0883 KOG0883 Cyclophilin type U box-containing peptidyl-prolyl cis-trans isomerase [Posttranslational modification protein turnover chaperones].

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 7 61 55 SSF50891 none none IPR029000
Gene3D 7 61 55 G3DSA:2.40.100.10 none none IPR029000
PANTHER 7 53 47 PTHR11071 none none IPR024936
Pfam 6 60 55 PF00160 none Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD IPR002130
PANTHER 7 53 47 PTHR11071:SF17 none none none

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
Bourran1_2004_QTL4_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,45 0 27,45 lod 4,5 10,6
Bourran_2000_2002_QTL7_Delta.F Qrob_Chr09 9 v_5944_442 s_1BA1PC_866 23.51 10,96 35,74 lod 4.1466 0.041
Bourran2_2003_QTL11_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 4,16 48,16 lod 2,3 5,1
Bourran2_2003_QTL13_peak_Bud_burst_A4 Qrob_Chr09 9 s_1AP8MN_635 s_1A3QQ_692 18,18 10,88 25,88 lod 3,4 7,2
Bourran2_2004_QTL12_peak_Bud_burst_3P Qrob_Chr09 9 s_1BDO6G_250 s_1A83AM_496 34,31 9,31 44,31 lod 3,6 7,6
Bourran2_2004_QTL14_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,83 10,33 22,33 lod 3,8 9
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_nSecLBD_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 35,81 34,88 37,45 lod 4.4 10.4
PM_1999_QTL15_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 9,16 47,16 lod 3,6 6,5

0 Targeting