(data stored in ACNUC8465 zone)

SWISSPROT: C1E1Z6_MICCC

ID   C1E1Z6_MICCC            Unreviewed;       256 AA.
AC   C1E1Z6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
DE   Flags: Fragment;
GN   ORFNames=MICPUN_72034 {ECO:0000313|EMBL:ACO61829.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61829.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61829.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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         Evidence={ECO:0000256|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; CP001324; ACO61829.1; -; Genomic_DNA.
DR   RefSeq; XP_002500571.1; XM_002500525.1.
DR   STRING; 296587.XP_002500571.1; -.
DR   GeneID; 8242184; -.
DR   KEGG; mis:MICPUN_72034; -.
DR   HOGENOM; HOG000161443; -.
DR   InParanoid; C1E1Z6; -.
DR   KO; K12737; -.
DR   OMA; FGRCVGD; -.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E1Z6.
DR   SWISS-2DPAGE; C1E1Z6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Isomerase {ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN       22    158       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
FT   NON_TER     256    256       {ECO:0000313|EMBL:ACO61829.1}.
SQ   SEQUENCE   256 AA;  28743 MW;  7A079AFEEA2932F5 CRC64;
     MSNVYQLEPP TEGKVLLTTS HGEIEVELWA KEAPKACRNF VQLCMEGYYD GCIFHRIIKD
     FMIQTGDPTG TGRGGESIYG EYFKDELHSR IKFNHRGQVA MANAGGRDTN GSQFFITLER
     TDWIDRKHTI FGKVTGHTIY NALQIADLEV DGDRPVEPYP KILKTEIVWN PFEDIVPRVM
     KKLDGDVDDE EAGDTRKKKK KEKKKLNLLS FGEEAGEEEE ELAKMAKPKV KSVFDADAAE
     NDGRIAKPGS AEEAAA
//

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