ID E6R8Q1_CRYGW Unreviewed; 366 AA.
AC E6R8Q1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN OrderedLocusNames=CGB_F6170W {ECO:0000313|EMBL:ADV23161.1};
OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV23161.1, ECO:0000313|Proteomes:UP000007805};
RN [1] {ECO:0000313|EMBL:ADV23161.1, ECO:0000313|Proteomes:UP000007805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WM276;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 0:0-0(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388}.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000256|ARBA:ARBA00010898}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000291; ADV23161.1; -; Genomic_DNA.
DR RefSeq; XP_003194948.1; XM_003194900.1.
DR AlphaFoldDB; E6R8Q1; -.
DR GeneID; 10190621; -.
DR KEGG; cgi:CGB_F6170W; -.
DR VEuPathDB; FungiDB:CGB_F6170W; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_012062_37_0_1; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000007805; Chromosome F.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
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 PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
FT DOMAIN 7..160
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 173..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 39743 MW; 890EE6017AC0B75D CRC64;
MPNTIAYFDI TIANEPAGRL IFELFDDVVP KTVNNFKHLC IGDKTNEAGV KLAYAGSSFH
RCIKGFMLQG GDFTRGDGTG GESIYGEKHE KPMLLSMANA GPGTNGSQFF ITTVPTPHLD
GKHVVFGRVM SNRSLVRRIE NIPTTSDRPN QPVTISSAGV LSPEEITQLE AERQAKQASS
EGGDIWEDWP QDEEGVDAEK PEEALAVAGK LKEVGTNEFK AGNFAVALDK YQKALRYLDV
HPVLPDDSPA ELVESFRSLR LPLLTNAALC ALKLPVSPNT SSLVVSLTSR ALTLPNLSAS
EKGKALYRRA QGYVLKKDDE AAEKDLKGAL ACVPGDAGVV RLLKDVEAKK KARKEKERQA
FAKMFG
//
