ID A4I4X6_LEIIN Unreviewed; 1081 AA.
AC A4I4X6; A0A2K4YZV7; A0A381MNG0;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAM69843.1};
GN ORFNames=LINJ_29_2790 {ECO:0000313|EMBL:CAM69843.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM69843.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM69843.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM69843.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM69843.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM69843.1,
RC ECO:0000313|Proteomes:UP000008153};
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR796461; CAM69843.1; -; Genomic_DNA.
DR RefSeq; XP_001466795.1; XM_001466758.1.
DR AlphaFoldDB; A4I4X6; -.
DR SMR; A4I4X6; -.
DR STRING; 5671.A4I4X6; -.
DR GeneID; 5070836; -.
DR KEGG; lif:LINJ_29_2790; -.
DR VEuPathDB; TriTrypDB:LINF_290034600; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; A4I4X6; -.
DR OMA; CCGRLFC; -.
DR OrthoDB; 125130at2759; -.
DR Proteomes; UP000008153; Chromosome 29.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11347:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT COILED 103..130
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 158..280
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 306..340
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 609
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 609..613
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 651
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 764
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 813
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1081 AA; 119669 MW; E7F5C8B3CC5037FF CRC64;
MSLMPGYPVP RAQWVESAEG CAACNKRFTF FTSKENCPCC GRLFCSSCLS AQCALFPTAP
PKAVCLDCFR KAQDWRLSQL EKQQQTSTQA DVGAATAPLS PSMAVLESKL SALEEEFYRA
KANARHLREE NDSLIDLLAA KDTCIAELRD KLMNGVSAGA AAQSAEKLQA ELQEAKDEKE
SMGRRLNEAE QRAAGAAQSS EAMRAQMQEH MQAKAEWESL EARLKSEARR AEHMLAQSLE
EMSELRAAMK STNAHSEEQI RQLTAQLQST VEANAHLQRD YDRNAEALRT AEQTRIASDA
HHDEELQRLR EHLATATAAL AQAQERYERE QRDTMKASDD AATAIAAEKQ REIDTLSEQL
ALSSAAAQRL QGELDRAIKE ATRLREEAAL KAEAANTLTS ELRTQLEAQG TAAQQEMPRQ
QEASVRLRAD LAEKEHLVMK LRRACRHAGT TARAQLDDLR GKLVETKVAY EEGQRSWQAW
LGELRAALEV VVQQGAVEVA ATSAPSTGAG MNGRGTTKSR WAQPTIIEEL QYPSVADVDV
RAIEPVPGLE LWEFDTVAEA QRGGEADVLL RVGHQIALDL HLFPDRASLH RWACLLATVQ
ANYRANQYHN RVHAADVLQG VYALICSCPG LLAHMTTVEK RAVVFAAAVH DIRHPGRSEI
FLKHTFDATY MHYNGLQVLE QMHTATAFHL LATPELDFTR GSMDDTEALE FHGLVAALIG
CTFMGRHASL MEQWSRPLQD GKTYDVTVTA DRQQVLSLLL HAADIGAQAR GLAVALKWLG
VVEEMRAQGD EEAARGLPLS PGSSRSASLE RGQIFFMEMF VVPLFDLVHQ MFPSIESPMR
NLRTVHAHYC AALQETRAFP PPVQYRTATQ PASNTAETSR AEALGTREAA VRKQEKAVEQ
SINRLREATA AVAGREKLLR EREVALMRAE TALKSQRLEK PSPTSSIGEE ELLRAITAIM
AREAEVQRRV ADVETMTAAL EERETIASRL SEQLASIADK INRRRQVLRY REARVRELEA
AFRGERGADF SSSDYITGPM CRAVAKPLST AAPLERMSPS SVQVVKLESA LEKLTSALRY
M
//
