ID   SSP1_NEUCR              Reviewed;         182 AA.
AC   O60045; Q7RVY7;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase ssp-1;
DE            Short=PPIase ssp-1;
DE            EC=5.2.1.8;
GN   Name=ssp-1; ORFNames=NCU08554;
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 [MRNA], AND CHARACTERIZATION.
RX   PubMed=9822668; DOI=10.1074/jbc.273.48.31971;
RA   Kops O., Eckerskorn C., Hottenrott S., Fischer G., Mi H., Tropschug M.;
RT   "Ssp1, a site specific parvulin homolog from N.crassa active in protein
RT   folding.";
RL   J. Biol. Chem. 273:31971-31976(1998).
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=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).
CC   -!- FUNCTION: Site-specific PPIase with respect to the amino acid N-
CC       terminal to the proline residue. Peptides with glutamate,
CC       phosphoserine, or phosphothreonine in the -1 position are the best
CC       substrates. It is not only able to isomerize small peptides but is also
CC       active in protein folding.
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;
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DR   EMBL; AJ006023; CAA06818.1; -; mRNA.
DR   EMBL; CM002238; EAA33800.2; -; Genomic_DNA.
DR   RefSeq; XP_963036.2; XM_957943.3.
DR   AlphaFoldDB; O60045; -.
DR   SMR; O60045; -.
DR   STRING; 5141.EFNCRP00000004618; -.
DR   EnsemblFungi; EAA33800; EAA33800; NCU08554.
DR   GeneID; 3879175; -.
DR   KEGG; ncr:NCU08554; -.
DR   VEuPathDB; FungiDB:NCU08554; -.
DR   HOGENOM; CLU_090028_0_0_1; -.
DR   InParanoid; O60045; -.
DR   OMA; DEVQCLH; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..182
FT                   /note="Peptidyl-prolyl cis-trans isomerase ssp-1"
FT                   /id="PRO_0000193434"
FT   DOMAIN          7..41
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          71..182
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   CONFLICT        167
FT                   /note="G -> D (in Ref. 1; CAA06818)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   182 AA;  20615 MW;  111D0497DFFF733A CRC64;
     MSNTIETGLP EDWEVRHSQS KNLPYYFNSA TKTSRWEPPS GTDVDKLKIY MAKYHSPTSQ
     QQQQQQQQQP QGKIRCAHLL VKHNQSRRPS SWRESEITRT KQEALTTLQG FEQRIKSGSI
     SLGELALTES DCSSARKRGD LGYFGRGDMQ KEFEDAAFAL KPGEISGIVD TASGLHLIER
     LE