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Database: UniProt
Entry: S3CIT5_OPHP1
LinkDB: S3CIT5_OPHP1
Original site: S3CIT5_OPHP1 
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
//
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