ID Q7S7Z6_NEUCR PRELIMINARY; PRT; 282 AA. AC Q7S7Z6; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 04-APR-2006, entry version 19. DE Hypothetical protein. GN ORFNames=NCU01200.1; OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=74-OR23-1A / FGSC 987; RX MEDLINE=22598136; 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., 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., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA 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., RA Paulsen I., 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: PPIases accelerate the folding of proteins (By CC similarity). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides (By similarity). CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. 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; AABX01000267; EAA32330.1; -; Genomic_DNA. DR UniGene; Ncr.5231; -. DR HSSP; P23284; 1CYN. DR SMR; Q7S7Z6; 30-198. DR GO; GO:0016853; F:isomerase activity; IEA. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA. DR GO; GO:0006457; P:protein folding; IEA. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Hypothetical protein; Isomerase; Rotamase. SQ SEQUENCE 282 AA; 30348 MW; 887F0E9F7FD9AADD CRC64; MFSLRRLLLA ATLFLGAMLL FAQSAEAAKG PKITHKVYFD IEQGDKPLGR IVMGLYGKTV PKTAENFRAL ATGEKGFGYE GSTFHRVIKQ FMIQGGDFTK GDGTGGKSIY GDKFPDENFK LKHSKKGLLS MANAGKDTNG SQFFITTVIT SWLDGKHVVF GEVLEGYDVV EKIENTKTGP RDAPAEPIKI AKSGELEVPP EGLEGQSEWA SPAYANEDEK PAAPVPVTDA KPPAHDSIPA ATADDDDTGA PLFAKVLFFG VLVLGLVLYI RLRRAPKGSG RA //