ID E3QCZ0_COLGM Unreviewed; 708 AA.
AC E3QCZ0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=GLRG_03906 {ECO:0000313|EMBL:EFQ28762.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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; GG697342; EFQ28762.1; -; Genomic_DNA.
DR RefSeq; XP_008092782.1; XM_008094591.1.
DR AlphaFoldDB; E3QCZ0; -.
DR STRING; 645133.E3QCZ0; -.
DR EnsemblFungi; EFQ28762; EFQ28762; GLRG_03906.
DR GeneID; 24409271; -.
DR VEuPathDB; FungiDB:GLRG_03906; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_1_1; -.
DR OrthoDB; 1334224at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000298; F:endopolyphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
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:UP000008782};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..708
FT /note="Endopolyphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003179623"
FT DOMAIN 53..318
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 385..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..685
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 79933 MW; 61F21553AD0703B7 CRC64;
MVGLLPLHLA LLQQFLHAVL ATPVASGQQI VLGPEAGDAD AVAPESSRRL HGKFLHITDF
HPDQFYKTHS STEEGLACHR GDGSAGYYGA ETSDCDAPSS LVNATFDWIA ANIADDIDFV
IWTGDTARHD SDEEIPRNPA QVLGTNRWVA DKFAETFGDP KDSTRMAVPV IPTFGNNDIL
PHNILLPGPN KWLGYYAEIW KRFIPEEQRH SFEYGGWFYV EVIPKKLAVF SLNTLYFFDR
NAGIDDCQQP SEPGFKQLEW LRVQLGFLRE RGMKAILMGH VPPARTDSKK NWDETCWQKY
NLWMQQYRDV VVGSLYGHMN IDHFIVHDTK DVNINILGGY AVDDDVGREA LDDELGIQSA
QDYLTELRQG WAKLPPVDAN ALEEDGSYDL EAQSKKGNKD KKKKKKPGKD LGGKYAERYH
LSFVGPSIVP NYFPTLRVME YNIAGLEDAS VWIDSFTKAA PSVLLSADDD HIYEDLKHDI
DAARKKKKKG KKGKKEKKPT PKDPNLVIPQ PPPAGTGPGP AYALQPLTFL GYTQYFANLT
YLNNDMTQET EDASGTRWRD GIHKDKDPKS KKPKPHPFAF EVEYSTFTDK IYKLSDLTVR
SYVKLANRLA KENAKGKALD EDFEEEDEDE EEELDDQKGT SDLGEEDDDG DEEVVDDEDG
IEVEKKKKNG GKKGKKGKKN KKKHNKVWLH FLKHAFVRTV PQKKLKKF
//
