ID   PPN1_KLULA              Reviewed;         681 AA.
AC   Q6CWT7;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Endopolyphosphatase;
DE            EC=3.6.1.10;
GN   Name=PPN1; OrderedLocusNames=KLLA0B01606g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic polyphosphate (polyP)
CC       chains of many hundreds of phosphate residues into shorter lengths.
CC       {ECO:0000250|UniProtKB:Q04119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate;
CC         Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10;
CC         Evidence={ECO:0000250|UniProtKB:Q04119};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q04119};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:Q04119};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04119}.
CC   -!- PTM: Processing by proteases in the vacuole may be required for
CC       activation. {ECO:0000250|UniProtKB:Q04119}.
CC   -!- SIMILARITY: Belongs to the endopolyphosphatase PPN1 family.
CC       {ECO:0000305}.
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DR   EMBL; CR382122; CAH01995.1; -; Genomic_DNA.
DR   RefSeq; XP_451602.1; XM_451602.1.
DR   AlphaFoldDB; Q6CWT7; -.
DR   SMR; Q6CWT7; -.
DR   STRING; 28985.XP_451602.1; -.
DR   EnsemblFungi; CAH01995; CAH01995; KLLA0_B01606g.
DR   GeneID; 2897267; -.
DR   KEGG; kla:KLLA0_B01606g; -.
DR   eggNOG; KOG3770; Eukaryota.
DR   HOGENOM; CLU_013424_1_0_1; -.
DR   InParanoid; Q6CWT7; -.
DR   OMA; MKAILMG; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000298; F:endopolyphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IEA:EnsemblFungi.
DR   CDD; cd00842; MPP_ASMase; 1.
DR   InterPro; IPR041805; ASMase/PPN1_MPP.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR012358; EndopolyPtase_N1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF027093; EndopolyPtase_N1; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..681
FT                   /note="Endopolyphosphatase"
FT                   /id="PRO_0000058547"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..681
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          549..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   681 AA;  78413 MW;  329D965217E51EEF CRC64;
     MKELQLPEKR KSNTGLSWFP SPRILQVFLV LLGAIVAFLS FSATSSIISS SPKHHSCHDN
     VEEAAVKYHY STISSDELPI SNERLASLGL TPNQPVKITD IGGKEKSIKG RFLHITDMHP
     DLYYKENTSI DDTCHRGKPK NDGDRAARFG NAMKGCDGPP DLMYYTLDWI HKNLSDEIDF
     IIWTGDNVRH DNDRRIPRTE QQIFDMNRQV SELFLKTFKD HESDDPRDLK VKIIPSLGNN
     DVFPHNLFSP GPTLQTRELY DIWSQFIPPA QQNTFDRYAS FFVEAIPGKL AVISLNTLYM
     FKGNPLVDNC SNKKQPGYKM LLWVGFTLQE LRDRGMKVWL SGHVPPIPKN FDSSCSDKLA
     LWLHEYSDII IGGFYGHMNM DHFIPVDGEK AWDDIANSMA ISEYSGFFEQ DFLEDAIAAR
     EIRAEGAKPV KKVNYMNGVR DAYYSRISED VKKLSEKDPL YERYSIVHIG TSIIPTFNPG
     FRIWEYNITE LQTEEEVLHS HQPWDSFFEH LDVEIQKIIE EAEEAEEVEA FEDDEQIDSE
     IPDVLISKKK KKKGKKGKKN KNSKNWWKTD KTFPKKKPKN LPPGPAYENQ LFSPLRFVQY
     YADLKEIDKQ YLKLLKEGKS EDEAASIAFK YQIEYASDDK PYPMKTTLVK DYIELASELS
     GNDKLWDTFL ERAFCSSGYE D