ID   CYPB_ARTBC              Reviewed;         226 AA.
AC   D4AY02;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable peptidyl-prolyl cis-trans isomerase ARB_01071 {ECO:0000305};
DE            Short=PPIase {ECO:0000250|UniProtKB:P14832};
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:P14832};
DE   AltName: Full=Rotamase {ECO:0000250|UniProtKB:P14832};
DE   Flags: Precursor;
GN   ORFNames=ARB_01071;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins (By similarity).
CC       Catalyzes the cis-trans isomerization of proline imidic peptide bonds
CC       in oligopeptides (By similarity). {ECO:0000250|UniProtKB:P14832}.
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:0000250|UniProtKB:P14832};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE32180.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000017; EFE32180.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003012820.1; XM_003012774.1.
DR   AlphaFoldDB; D4AY02; -.
DR   SMR; D4AY02; -.
DR   STRING; 663331.D4AY02; -.
DR   EnsemblFungi; EFE32180; EFE32180; ARB_01071.
DR   GeneID; 9522898; -.
DR   KEGG; abe:ARB_01071; -.
DR   eggNOG; KOG0880; Eukaryota.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; 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   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Isomerase; Reference proteome; Rotamase; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..226
FT                   /note="Probable peptidyl-prolyl cis-trans isomerase
FT                   ARB_01071"
FT                   /id="PRO_0000434908"
FT   DOMAIN          38..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          194..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   226 AA;  24764 MW;  4D563B4943B27F12 CRC64;
     MARIGRILTL VVFAAVGLFL FMGQTVEAKG PKITSKVYFD IEHDGQPLGR IVMGLYGKTV
     PKTAENFRAL ATGEKGFGYE GSTFHRVIKD FMIQGGDFTN GDGTGGKSIY GNKFEDENFK
     LRHTKKGVLS MANAGKDTNG SQFFITTAIT AWLDGKHVVF GEVLEGYDIV DKIQVVPKGF
     QDRPTKDVKI VKCGELDMKE EAEGEGTESP SKPDSEKEQA PVRDEI