ID A5DAS6_PICGU Unreviewed; 602 AA.
AC A5DAS6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Endopolyphosphatase {ECO:0000256|ARBA:ARBA00014458, ECO:0000256|PIRNR:PIRNR027093};
DE EC=3.6.1.10 {ECO:0000256|ARBA:ARBA00012459, ECO:0000256|PIRNR:PIRNR027093};
GN ORFNames=PGUG_00381 {ECO:0000313|EMBL:EDK36283.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36283.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK36283.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic polyphosphate (polyP)
CC chains of many hundreds of phosphate residues into shorter lengths.
CC {ECO:0000256|PIRNR:PIRNR027093}.
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:0000256|PIRNR:PIRNR027093};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004576}.
CC -!- SIMILARITY: Belongs to the endopolyphosphatase PPN1 family.
CC {ECO:0000256|ARBA:ARBA00010399}.
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; CH408155; EDK36283.2; -; Genomic_DNA.
DR RefSeq; XP_001487004.1; XM_001486954.1.
DR AlphaFoldDB; A5DAS6; -.
DR STRING; 294746.A5DAS6; -.
DR GeneID; 5129172; -.
DR KEGG; pgu:PGUG_00381; -.
DR VEuPathDB; FungiDB:PGUG_00381; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_1_1; -.
DR InParanoid; A5DAS6; -.
DR OMA; WAERYSV; -.
DR OrthoDB; 1334224at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000298; F:endopolyphosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 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 PANTHER; PTHR10340:SF59; METALLOPHOS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF027093; EndopolyPtase_N1; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR027093};
KW Membrane {ECO:0000256|PIRNR:PIRNR027093};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|PIRNR:PIRNR027093}.
FT DOMAIN 50..286
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 602 AA; 69303 MW; B793F71CB03A9583 CRC64;
MRVPQVLQWS CMAVACAAHI TQETPLSLAE LGLTETTPIT LSNNHKLHGR FLHITDMHPD
PYYEEGAFQS ELCHVGKDKD AKKGDAGKYG DAVSGCDSPM ILMNETLAWI SKHLRDKIDF
VVWTGDNIRH DNDRRYPRTE THIFDMNQLV SDYVVDTFRS DNNYGSPLGI PVVPSLGNND
VYPHNLFAKG PTLQTREMFK IWQPFIPPEQ LHVFSRGAYF FKEVIPNKLA VLSINTLYLF
QSNPLVDNCD RKKEPGYMLF KWLGYVLKEM RARKMKVWLS GHVPPNEKNY DISCLRKYIM
WTHEYRDVIV GGLYGHMNID HFIPLDAKAA YKSLDAKYGG VQVPFADEEV SFEDDSLEGS
YRRLGYSIWD DSIDGNFDQL PKFSSFNDVR IAGGIPNNKV RYMETIRDEV YRDISRRKKQ
GEFSERYAVA HVTASIVPTF NPGIRVWEYN TTGLDTKSDI EYAPWDEFFS GLEQLLQNNE
NHDDNDLHTL KRDKTFPPKM PKDLPLGPAY VPQAFTPTRY VQYYADLKAI NKGDKKFGYE
IEYTTDDKDH QMSPLTVDQW MKYGRKLAKA GKKKASNKEK RMWNAFLHQA FVSSGYEDMG
LG
//
