ID   CYP9_CAEBR              Reviewed;         313 AA.
AC   A8X8D0; Q9XTP5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 9;
DE            Short=PPIase 9;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-9;
DE   AltName: Full=Rotamase 9;
GN   Name=cyn-9 {ECO:0000250|UniProtKB:Q09637};
GN   Synonyms=cyp-9 {ECO:0000312|EMBL:CAB40206.1}; ORFNames=CBG09202;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAB40202.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-249, AND NUCLEOTIDE SEQUENCE [MRNA]
RP   OF 1-141.
RX   PubMed=10216266; DOI=10.1016/s0378-1119(99)00102-x;
RA   Page A.P.;
RT   "A highly conserved nematode protein folding operon in Caenorhabditis
RT   elegans and Caenorhabditis briggsae.";
RL   Gene 230:267-275(1999).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imid ic peptide bonds in
CC       oligopeptides. Thought to function as a catalyst in the folding and
CC       modification of cuticle collagens (By similarity).
CC       {ECO:0000250|UniProtKB:Q09637}.
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:0000250|UniProtKB:Q09637};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB40202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; HE601123; CAP28891.2; -; Genomic_DNA.
DR   EMBL; AJ005807; CAB40202.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AJ005809; CAB40206.1; -; mRNA.
DR   AlphaFoldDB; A8X8D0; -.
DR   SMR; A8X8D0; -.
DR   STRING; 6238.CBG09202; -.
DR   EnsemblMetazoa; CBG09202.1; CBG09202.1; WBGene00030832.
DR   WormBase; CBG09202; CBP25106; WBGene00030832; Cbr-cyn-9.
DR   eggNOG; KOG0546; Eukaryota.
DR   HOGENOM; CLU_012062_33_4_1; -.
DR   InParanoid; A8X8D0; -.
DR   OMA; HCNGKHV; -.
DR   OrthoDB; 1403619at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..313
FT                   /note="Peptidyl-prolyl cis-trans isomerase 9"
FT                   /id="PRO_0000332946"
FT   DOMAIN          9..174
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          216..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  35787 MW;  06AA294B751FFCA3 CRC64;
     MSSLEKRVFL DMALDEKPIG RIEIKLFTSE APKTCENFRA LCTGEVGMAP NNKARLHYKG
     NEIHRVVKKF MIQGGDITDG DGRGGFSIYG RYFDDEKFVL KHSKPYLLSM ANKGPNSNSS
     QFFITTAPAP HCNGKHVVFG EVIKGREVVD VLDNLEVDGK SKPIAKVRIF NSGELVKKKK
     PSKTKEELAA LEERKRQEAK KDIPDIPKSW LYRDNEERES DFSSKTESSR VRSRSKSPSN
     NYETRRGHMA NSRGDRNRRT QRADRKDDFG IAVRGRGGVQ FRRVRYVTPE HWRRNAPSKW
     QQGSYTHPVD LQP