ID M2X3D0_GALSU Unreviewed; 360 AA.
AC M2X3D0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=Gasu_19080 {ECO:0000313|EMBL:EME30895.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30895.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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, ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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DR EMBL; KB454496; EME30895.1; -; Genomic_DNA.
DR RefSeq; XP_005707415.1; XM_005707358.1.
DR AlphaFoldDB; M2X3D0; -.
DR STRING; 130081.M2X3D0; -.
DR EnsemblPlants; EME30895; EME30895; Gasu_19080.
DR GeneID; 17089589; -.
DR Gramene; EME30895; EME30895; Gasu_19080.
DR KEGG; gsl:Gasu_19080; -.
DR eggNOG; KOG0549; Eukaryota.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR45779:SF6; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:EME30895.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..222
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 360 AA; 41767 MW; 4229C0B1C8C97228 CRC64;
MKKRLKQRKQ PTWLLQQRAF LVTACIAVLY GIYIRINYQS NSEETSAFIS YFEDFLQSHQ
QRDWIDTSDL FVRTESNDNP WNLAFLKERY PNVDLSWNKL EDPKTFKRKG VIVHKHRNVV
GCGGTYVAGA SWGDFVHLRF IGKLDNGTVF DSTRGRKQLF RFQLGWKNIS RGWNIGLLGM
CPGEIRELVI TSKLFSNDEK NLYFPNWKDR KLYYLIQLVC IGEDASPPEH HFRQWKDPYE
LLREHTVIIP AKRKQNCYRA CQLKNLVCFK KGFSILNNCP TLSEYFDCRE CEIATMESAG
SDMPCRVSLK APSTYSSGVC MISPNLSLTS CEASHSQTER LCPCVVATDM LLEKTQYLRI
//
