ID E9AC11_LEIMA Unreviewed; 335 AA.
AC E9AC11;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Putative cyclophilin 12 {ECO:0000313|EMBL:CBZ11825.1};
DE EC=5.2.1.8 {ECO:0000313|EMBL:CBZ11825.1};
GN Name=CYP12 {ECO:0000313|EMBL:CBZ11825.1};
GN ORFNames=LMJF_01_0220 {ECO:0000313|EMBL:CBZ11825.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CBZ11825.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=10077609; DOI=10.1073/pnas.96.6.2902;
RA Myler P.J., Audleman L., deVos T., Hixson G., Kiser P., Lemley C.,
RA Magness C., Rickel E., Sisk E., Sunkin S., Swartzell S., Westlake T.,
RA Bastien P., Fu G., Ivens A., Stuart K.;
RT "Leishmania major Friedlin chromosome 1 has an unusual distribution of
RT protein-coding genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2902-2906(1999).
RN [2] {ECO:0000313|EMBL:CBZ11825.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [3] {ECO:0000313|EMBL:CBZ11825.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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DR EMBL; FR796397; CBZ11825.1; -; Genomic_DNA.
DR RefSeq; XP_003721542.1; XM_003721494.1.
DR AlphaFoldDB; E9AC11; -.
DR STRING; 5664.E9AC11; -.
DR EnsemblProtists; CBZ11825; CBZ11825; LMJF_01_0220.
DR GeneID; 12983115; -.
DR KEGG; lma:LMJF_01_0220; -.
DR VEuPathDB; TriTrypDB:LmjF.01.0220; -.
DR VEuPathDB; TriTrypDB:LMJFC_010007300; -.
DR VEuPathDB; TriTrypDB:LMJLV39_010007100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_010007200; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_830165_0_0_1; -.
DR InParanoid; E9AC11; -.
DR OMA; VITDCDV; -.
DR Proteomes; UP000000542; Chromosome 1.
DR GO; GO:0005930; C:axoneme; ISO:GeneDB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:CBZ11825.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT DOMAIN 153..330
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 59..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 36187 MW; EF81535EC1AA35FE CRC64;
MKGVTSFTVY GLVPAADFQR CAEAAAYVND KYPESYAVIV KLELPRDFAE RRAAWASAGH
LPSQQQQPTD ASFGESGGSA TTASTAAAEL AAVLVEQHGS DSEPQCLLTA ETFLHNIATH
TDYKPDATED YYTARGKRAW RAFLASRGRQ YCWMDVSVDG VAVGRVWFEL YASVAPLTCK
NFCELCRGTT VAMGDTVAHS SVFDPPPAQH IGYKGTTFFR TLKDAWVMGG DVTGAHSGNG
GYSCYGRCFP DETYAVPHDA AGILGMCNDG PHTSSSAFYI TLRPMSWMNG KYVAFGRVMD
GMHVVDAIHA VEARHNQAPK ASIVITDCDV LDTSV
//
