ID M4C143_HYAAE Unreviewed; 485 AA.
AC M4C143;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=PPIase cyclophilin-type domain-containing protein {ECO:0000259|PROSITE:PS50072};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP812772, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP812772}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP812772};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JH598089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4C143; -.
DR STRING; 559515.M4C143; -.
DR EnsemblProtists; HpaT812772; HpaP812772; HpaG812772.
DR VEuPathDB; FungiDB:HpaG812772; -.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_4_1; -.
DR InParanoid; M4C143; -.
DR OMA; NDDKSWM; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF6; SPLICEOSOME-ASSOCIATED PROTEIN CWC27 HOMOLOG; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713}.
FT DOMAIN 1..119
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 55035 MW; 91346FFD0A21D339 CRC64;
MVQGGDPTGT GNGGESIYGG AFIDEFHSRL RFNHRGLLAM ANENKPNSNH SQFFFTLDAC
DFLDKKHTIF GKVRRVERRR TVRLKVTGNT IFNMLSVGDL ETNEQDRPIH PPRLLSVEVL
WNPFEDIVSR AVKRDEMSSA NDSQEKNKQK RKATKDLKLL SFGDDEEAFQ EEIAGSAKTL
KKKAKTMMSS HDLLGDQKLK AEVDAKVLQK VAETNGAATS EDKKARAREK LKAAVAAASN
KTDSSEKGRD ASNNLDTTNG DKFSASSSRQ KIDREEYAKL REELRKSKKA VPLLMGEEAK
KLDEGRAFQD MLTPLQQQRQ KYLQRKKSSK RSTREQETLM KLKRFQTTLI SVNSKNTNLA
NDADAKSDET KTDIIESYHG QILENDDEHD DTNDDKSWMT AKLKFKKHID VSYSHCIGVS
GSLCYKTVLT VLYRLRIPQD QFRSGHDPSA DDYMTIDSRN KREQRSSGDS RRNRSQDRSR
GSRRP
//
