ID A0A1Z5K093_FISSO Unreviewed; 425 AA.
AC A0A1Z5K093;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=FisN_4Lh392 {ECO:0000313|EMBL:GAX19411.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX19411.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX19411.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX19411.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SYF2 family.
CC {ECO:0000256|ARBA:ARBA00010028}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX19411.1}.
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DR EMBL; BDSP01000136; GAX19411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5K093; -.
DR InParanoid; A0A1Z5K093; -.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR013260; mRNA_splic_SYF2.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF08231; SYF2; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 4..159
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 166..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47479 MW; 2D71C3BDC13FF354 CRC64;
MKAYMTFQHG SQPLGILYME LEPKVVPKTV RNFETFLRKG YKGTNVHRLI KGFMLQAGDI
TAGDGTGGYS IYGKTFADEN FILRHDRPGR LSMANAGPNT NGSQFFITFK PTPHLDGKHV
VFGSVDLQRS GALLKTLEQI KTLSNDKPKQ ELTIVDCGIL EEASNSAKTT AVAEAADVDA
DEIDLEEEED VETGNDVVEE VVEPEEEEEE EDSKPLSKSE ALKRRLRKLK QKVNQARQLN
KQAVKDEGER STDEGSASAR KKLAASNKEG KNFIWAQQNA KALSIANESG VDAKHLTEQA
VDSVYKARLA AERAETQPHK YLRDLKSIPR NLPQSSETGI LTFNPLQNEV NPDKEREGAR
RLALEMHKRV EKNTKRLLSV KRKGGDGGDV SYINKRNKIF NEKISRDYDK HTAEIRESLE
RGSAL
//
