ID S3CIT5_OPHP1 Unreviewed; 721 AA.
AC S3CIT5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=F503_02431 {ECO:0000313|EMBL:EPE06303.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE06303.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE06303.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE06303.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148153; EPE06303.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CIT5; -.
DR STRING; 1262450.S3CIT5; -.
DR VEuPathDB; FungiDB:F503_02431; -.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_013424_1_1_1; -.
DR OMA; WAERYSV; -.
DR OrthoDB; 1334224at2759; -.
DR Proteomes; UP000016923; 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:SF55; ENDOPOLYPHOSPHATASE; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR027093};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR027093};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|PIRNR:PIRNR027093}.
FT DOMAIN 91..351
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 80965 MW; D311036760A6131D CRC64;
MQSHTSRRLR TSKSSSSSST SRAMTLTRLV PLLLCSTAAL AGPLRLPQFA RPRLGSPNEH
DQPQRVLGSI ADADISSPAK TEAGQRKLHG KFLHITDFHP DEFYKAHSST SAENACHSGN
GPAGTYGAET SDCDTPYTLV NATFDWIREN IRDEIDFVIW TGDSARHDSD ESIPRSPAQV
QDSNEFIANK FIDLLEDPSG QGLIVPVIPT LGNNDILPHN VLLPGPNKWL KRYTDIWNRF
IPQEQRHSFE FGGWFYVEVI PNRLAVFSLN SLYFFDRNAG VDDCVNPTEP GFKQLEWLRI
QLQFMRERGV KAILMGHVPP ARTGSKQLWD ETCWQKYTLW LRQYRDVIVS GLYGHMNIDH
FMLQDAKDLD YNFLGAEAFL EEEDDDDFDD DDFFAEDASE TIVRASMEDE MGIQSTADYL
QELRSGWAKL PKPTTAQVTG SGEVDAEKKK RKKKKGKKGR SPRLSKKWSE RYQLSFVAPS
IVPNYLPSLR VMEYNISGLE NAPIWTDGPL SVPFISADDL LAKNVLGGGV EAQKKKKKGK
KDKKKGKKDP NLVVPQGPSK TAVPGPAYSP QTLTLLGYTQ YFANLTYINN DMTTDEEEID
PDSVDSVDSL KWREGKHGDK EPKKGKPHKF QFKVEYSTFT DKIYGLTDMT VNSLLEMAYR
MGKKKAKTGS IDVEGNEAGV SADVPATDEV STTKTNEVWL HFLRHAFVSS VSPEELEKLD
S
//