ID C1G6Q2_PARBD Unreviewed; 688 AA.
AC C1G6Q2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=PADG_02857 {ECO:0000313|EMBL:EEH46759.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH46759.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH46759.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH46759.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR EMBL; KN275959; EEH46759.1; -; Genomic_DNA.
DR RefSeq; XP_010758628.1; XM_010760326.1.
DR AlphaFoldDB; C1G6Q2; -.
DR STRING; 502780.C1G6Q2; -.
DR GeneID; 22582268; -.
DR KEGG; pbn:PADG_02857; -.
DR VEuPathDB; FungiDB:PADG_02857; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_1_1; -.
DR InParanoid; C1G6Q2; -.
DR OMA; WAERYSV; -.
DR OrthoDB; 1334224at2759; -.
DR Proteomes; UP000001628; 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.
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:UP000001628};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|PIRNR:PIRNR027093}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..688
FT /note="Endopolyphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002909838"
FT DOMAIN 44..293
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 474..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..501
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 78459 MW; E68E2BEB864CA2BB CRC64;
MSKLIVTISF LAVWPLQGFA GALYPLALEP GKVRVERDQK LHGRFLHITD IHLDTYYKPH
SNPDDDHECH RGPGNAGYFG TTGSSCDSPL ALVDATFAWI QENVADSIDF VVWTGDSARH
DNDEKAPRTE KEVIDMNQVL ADKFFDIFSK SSGKENGMRI PVVPTIGNND IMPHNIFKSG
PNRWTRKLGM IWDPFIPEEQ RHTFVEGGWF YVEVIPDKLA VFSLNTLYFY DSNSAADGCE
DKNEPGYKHM EWLRVQLQFI RKRNMKAILI GHVPPARTDS KENWDETCWQ KYTLWLYQYR
DIIVGNMFGH MNIDHFMFQD SKELKFGYDG VESHHKQGKQ QGAEEKVSVQ SRLAYLSSLR
RDWSQLPYPP EPSPSSFVFI NDSHHNDDIH LLDSSSSRKK KRMGEYLNEI GGPWAERYSV
SLVSPSIIPN YYPALRVIEY NTSGLENASL WSEVSGQHNK PSFRTSTLSE DLDFEGQNLS
AKKKKGSKKK KKKKKKKPTF KVPHPPSPTA PPGPAYSNQP FTLLSYTQYF SNLSDIDTKT
MVSTANQYSD NQNPLHWIRG RGRKPDRYEP RSISFEVLYD TKTDKSYKLK DLTVRSYLDL
ARRVAQKDSE KKDQPLVLPN ADARCQQRKA ETPDGPSGPP LDAGGDKSDP LCTQIELPLS
AGTKSRESIW AVFVRRAFVG YFDSDVMQ
//
