PIN1_RHIO9
ID PIN1_RHIO9 Reviewed; 150 AA.
AC P0C1J8; I1BIC9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase pin1;
DE Short=PPIase pin1;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin pin1;
GN Name=pin1; ORFNames=RO3G_00663;
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Catalyzes pSer/Thr-Pro cis/trans isomerizations (By
CC 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 PpiC/parvulin rotamase family.
CC {ECO:0000305}.
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DR EMBL; CH476732; EIE75959.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C1J8; -.
DR SMR; P0C1J8; -.
DR STRING; 936053.P0C1J8; -.
DR EnsemblFungi; EIE75959; EIE75959; RO3G_00663.
DR VEuPathDB; FungiDB:RO3G_00663; -.
DR eggNOG; KOG3259; Eukaryota.
DR InParanoid; P0C1J8; -.
DR OMA; DEVQCLH; -.
DR OrthoDB; 1437969at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..150
FT /note="Peptidyl-prolyl cis-trans isomerase pin1"
FT /id="PRO_0000244731"
FT DOMAIN 1..35
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 39..150
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ SEQUENCE 150 AA; 17389 MW; 7BD9B0658FF92074 CRC64;
MDLPENWIVR HSRTYNKDYY YNTVTNESRW DAPVLKGELE RVRASHLLIK SRESRRPSSW
REEHITRSKE EALKILTDFQ HKIESGQETL SALATNYSDC TSAKRGGDLG YFERGQMQKP
FEEATFALQV GELSKPVWTD SGVHLILRTA
