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Database: UniProt
Entry: C4Y875_CLAL4
LinkDB: C4Y875_CLAL4
Original site: C4Y875_CLAL4 
ID   C4Y875_CLAL4            Unreviewed;       359 AA.
AC   C4Y875;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=CLUG_04403 {ECO:0000313|EMBL:EEQ40275.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40275.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ40275.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40275.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
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DR   EMBL; CH408080; EEQ40275.1; -; Genomic_DNA.
DR   RefSeq; XP_002615521.1; XM_002615475.1.
DR   AlphaFoldDB; C4Y875; -.
DR   STRING; 306902.C4Y875; -.
DR   GeneID; 8496219; -.
DR   KEGG; clu:CLUG_04403; -.
DR   VEuPathDB; FungiDB:CLUG_04403; -.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; C4Y875; -.
DR   OMA; QFFITTY; -.
DR   OrthoDB; 1994238at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00317; cyclophilin; 1.
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; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
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; PF07719; TPR_2; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          5..154
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REPEAT          297..330
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   359 AA;  40252 MW;  A6CE4396B22521EA CRC64;
     MSNVYLDVSI GGTPCGRIVL SLDHEKAPLA CEHFCSNLPR YTDTYFHRVI KNFVIQGGDV
     VFGHKDQYGD ASVGTGKEDF FPDENLQAPL DKPFQLCMAN SGPNTNSTQF FISTYPTPHL
     QGKHTVFGRV IHGKSVVRAI ERVKTNAANV PAKEELPVIT ETGTWRDGNA IPIFNACYDT
     VGGDIYEEYP DDDEHIDKDS SSSVYDAACA IKNSGAALFK RGEFQNAMFK YTKALRYVME
     YIPDEDQEPD FHAKYSELKK KLYLNVSLVA LKLGDNVKCV DYGSYLLEMT LTPQEKAKVY
     YRMGCAYSAQ RKYKEAISSL EKARALASDV GIEHELKKAK ELQDAQIQKE KAKYAKFFG
//
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