ID PPIH_NEUCR Reviewed; 182 AA.
AC Q7SG06;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE Short=PPIase H;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase H;
GN Name=cyp-3; ORFNames=53H1.080, NCU02614;
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=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 [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: 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC subfamily. {ECO:0000305}.
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DR EMBL; CM002236; EAA35781.1; -; Genomic_DNA.
DR EMBL; BX842633; CAE76450.1; -; Genomic_DNA.
DR RefSeq; XP_965017.1; XM_959924.2.
DR AlphaFoldDB; Q7SG06; -.
DR SMR; Q7SG06; -.
DR STRING; 367110.Q7SG06; -.
DR PaxDb; 5141-EFNCRP00000002116; -.
DR EnsemblFungi; EAA35781; EAA35781; NCU02614.
DR GeneID; 3881157; -.
DR KEGG; ncr:NCU02614; -.
DR VEuPathDB; FungiDB:NCU02614; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; Q7SG06; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..182
FT /note="Peptidyl-prolyl cis-trans isomerase H"
FT /id="PRO_0000232958"
FT DOMAIN 15..181
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 182 AA; 19734 MW; 15E84C8374BE790F CRC64;
MAPTVLPASG NPLVFFDITL GGEPLGRITF ELFKDVVPRT AENFRQFCTG ESKNNLGRPQ
GYKGSKFHRI IPNFMCQGGD FLNGDGTGST CIYGTKSFAD ENFLLKHDTP GLLSMANAGP
NTNGSQFFIT TVPTPFLDGK HVVFGKVVDG MDVVKKMENT KTGYRGKDVP NLDVVIAQCG
EM
//
