ID A0A067CGT1_SAPPC Unreviewed; 428 AA.
AC A0A067CGT1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=PPIase cyclophilin-type domain-containing protein {ECO:0000259|PROSITE:PS50072};
GN ORFNames=SPRG_06638 {ECO:0000313|EMBL:KDO28400.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO28400.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO28400.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO28400.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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DR EMBL; KK583211; KDO28400.1; -; Genomic_DNA.
DR RefSeq; XP_012200842.1; XM_012345452.1.
DR AlphaFoldDB; A0A067CGT1; -.
DR STRING; 695850.A0A067CGT1; -.
DR EnsemblProtists; KDO28400; KDO28400; SPRG_06638.
DR GeneID; 24128973; -.
DR KEGG; spar:SPRG_06638; -.
DR VEuPathDB; FungiDB:SPRG_06638; -.
DR OMA; PFYNKTM; -.
DR OrthoDB; 47446at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR CDD; cd03419; GRX_GRXh_1_2_like; 2.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR PANTHER; PTHR45694:SF18; GLUTAREDOXIN-1-RELATED; 1.
DR Pfam; PF00462; Glutaredoxin; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..209
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 428 AA; 46465 MW; 9F127983B0D05B6A CRC64;
MLPHHKSRRP APSAGAMAYL PYGLGAIFTL AVLKFLFFFD PIPLEDMLPF VNKTMYKVST
LHGDFVLELF PDAAPRTVAH FEKLVAAGFY TKDAGFYRAE PDFLVQAGGF VHDKPSPFGT
VDVEYNLPSE ERTLVLARSA DPSSGSTEFS IMLTDNTAIN APSDTSPGYT VFGRVHAGYP
NVKLLADVMS EGYLAKKNRH QAIAFDAIEK ITALVPTTLE LRLVSDAIHD ALAARFSVVM
FGKTTCPYCK KAKAILKELK AEVLVVEIDL LPPAVMSQYQ DMLEALTGRR TVPNILLNGQ
SIGGGDDVEA LHQSKKLAPM LQKVGALAKA VVLDSITTNP LVIFTKSFDP YSKDVKKLFK
SLGAKAVVIE IDTRDDGNAI LYNLQKLTGR KTTPNVFVAG KTIGGCDDTK ALHETGELTL
LLQQAGAL
//