PIN4_NEUCR
ID PIN4_NEUCR Reviewed; 130 AA.
AC Q7RYY4; U9W4J5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase pin4;
DE Short=PPIase pin4;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin-14;
DE Short=Par14;
GN Name=ppi-5; Synonyms=pin4; ORFNames=NCU06433;
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 [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 [2]
RP REVISION OF GENE MODEL.
RA Pemberton T.J.;
RL Submitted (FEB-2006) to UniProtKB.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily. {ECO:0000305}.
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DR EMBL; CM002238; ESA43163.1; -; Genomic_DNA.
DR EMBL; CM002238; ESA43164.1; -; Genomic_DNA.
DR RefSeq; XP_011393912.1; XM_011395610.1.
DR RefSeq; XP_011393913.1; XM_011395611.1.
DR AlphaFoldDB; Q7RYY4; -.
DR SMR; Q7RYY4; -.
DR STRING; 5141.EFNCRP00000006264; -.
DR EnsemblFungi; ESA43163; ESA43163; NCU06433.
DR EnsemblFungi; ESA43164; ESA43164; NCU06433.
DR GeneID; 3873493; -.
DR KEGG; ncr:NCU06433; -.
DR VEuPathDB; FungiDB:NCU06433; -.
DR HOGENOM; CLU_090028_2_0_1; -.
DR InParanoid; Q7RYY4; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR043323; PIN4.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR PANTHER; PTHR45995; PTHR45995; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..130
FT /note="Peptidyl-prolyl cis-trans isomerase pin4"
FT /id="PRO_0000232935"
FT DOMAIN 36..128
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 130 AA; 13658 MW; C766D3387387D8DF CRC64;
MGKDKKASGS GSGSKGGKDA GNKDAGKDAG KASKGAQSIN VRHILCEKHG KKEEALAKIR
DGADFGAVAR EYSEDKARTG GSLGWKQKGT LDPEFEKVAF ALETSSTSSP KIGEVKTQFG
YHIIMVEGKK