ID   FKB1A_NEUCR             Reviewed;         120 AA.
AC   P20080; Q7S7U2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=FK506-binding protein 1A;
DE            Short=FKBP-1A;
DE            EC=5.2.1.8;
DE   AltName: Full=FK506-resistance protein 2;
DE   AltName: Full=NcFKBP13;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase fkr-2;
DE            Short=PPIase fkr-2;
GN   Name=fkr-2; ORFNames=9G6.180, NCU04140;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1696687; DOI=10.1038/346674a0;
RA   Tropschug M., Wachter E., Mayer S., Schoenbrunner E.R., Schmid F.X.;
RT   "Isolation and sequence of an FK506-binding protein from N. crassa which
RT   catalyses protein folding.";
RL   Nature 346:674-677(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-39.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=11034311; DOI=10.1016/s0014-5793(00)01901-3;
RA   Solscheid B., Tropschug M.;
RT   "A novel type of FKBP in the secretory pathway of Neurospora crassa.";
RL   FEBS Lett. 480:118-122(2000).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Binds to the immunosuppressant drug FK506.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA32060.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X55743; CAA39274.1; -; Genomic_DNA.
DR   EMBL; AL513463; CAC28766.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32060.2; ALT_INIT; Genomic_DNA.
DR   PIR; S11090; S11090.
DR   RefSeq; XP_961296.2; XM_956203.3.
DR   AlphaFoldDB; P20080; -.
DR   SMR; P20080; -.
DR   STRING; 5141.EFNCRP00000003914; -.
DR   EnsemblFungi; EAA32060; EAA32060; NCU04140.
DR   GeneID; 3877460; -.
DR   KEGG; ncr:NCU04140; -.
DR   HOGENOM; CLU_013615_8_1_1; -.
DR   InParanoid; P20080; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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; PTHR45779; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Isomerase; Reference proteome;
KW   Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11034311"
FT   CHAIN           2..120
FT                   /note="FK506-binding protein 1A"
FT                   /id="PRO_0000075303"
FT   DOMAIN          26..114
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   120 AA;  13037 MW;  AF97183C041563B7 CRC64;
     MTIPQLDGLQ IEVQQEGQGT RETRRGDNVD VHYKGVLTSG KKFDASYDRG EPLNFTVGQG
     QVIKGWDEGL LGMKIGEKRK LTIAPHLAYG NRAVGGIIPA NSTLIFETEL VGIKGVQKGE