YGK5_SCHPO
ID YGK5_SCHPO Reviewed; 485 AA.
AC O94323;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Uncharacterized pyrophosphatase/phosphodiesterase C725.05c;
DE EC=3.-.-.-;
GN ORFNames=SPBC725.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22177.1; -; Genomic_DNA.
DR PIR; T40657; T40657.
DR RefSeq; NP_595485.1; NM_001021396.2.
DR AlphaFoldDB; O94323; -.
DR SMR; O94323; -.
DR BioGRID; 277691; 34.
DR STRING; 4896.SPBC725.05c.1; -.
DR iPTMnet; O94323; -.
DR MaxQB; O94323; -.
DR PaxDb; O94323; -.
DR PRIDE; O94323; -.
DR EnsemblFungi; SPBC725.05c.1; SPBC725.05c.1:pep; SPBC725.05c.
DR GeneID; 2541177; -.
DR KEGG; spo:SPBC725.05c; -.
DR PomBase; SPBC725.05c; -.
DR VEuPathDB; FungiDB:SPBC725.05c; -.
DR eggNOG; KOG2645; Eukaryota.
DR HOGENOM; CLU_017594_1_2_1; -.
DR InParanoid; O94323; -.
DR OMA; VMAWFTE; -.
DR PhylomeDB; O94323; -.
DR Reactome; R-SPO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-SPO-196843; Vitamin B2 (riboflavin) metabolism.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-6814848; Glycerophospholipid catabolism.
DR PRO; PR:O94323; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IBA:GO_Central.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISO:PomBase.
DR GO; GO:0004551; F:nucleotide diphosphatase activity; ISO:PomBase.
DR GO; GO:0009141; P:nucleoside triphosphate metabolic process; ISO:PomBase.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..485
FT /note="Uncharacterized pyrophosphatase/phosphodiesterase
FT C725.05c"
FT /id="PRO_0000317129"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 74..404
FT /note="Phosphodiesterase"
FT /evidence="ECO:0000250"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 485 AA; 55149 MW; A739B5CF4F5582CA CRC64;
MFSWANIGSN EYLPLKNDRK AYLNQWAKRS GLAIAAICIL GILILAIVKL FCFKAIIFPI
VGGSFNNGTN VFQSTVIVIS LDGFRADYLY RGFTPNLLSL AERNVHVPFL IPSFPSITFP
NHYTIVTGLY PESHGIVSNN FFDPVTGKQF VNSMPECNKD PTWWDKGEPI WVNAERNNVR
SAVHMWPGNE VENHGYRPTY SDGFNFDTTL REKKDRILEW LDLPDKDRPQ LLLAYAPHVD
MVGHAFGPDS PELNIIIQEV DIVIGELIEG LKKRNIDKHV NIIFLSDHGM APTSDNRLIW
LDNMFNLSAV AHRDAWPLGG FRGESDLDDE YIYESLVNYS RSSLPSAENW NVYSKKDIPS
RWHYSNNERI APVWMIPDVG WSLVSMLDHS PELEYEPLGV HGYDNLSPVM RALFIASGSS
FKNFKGKKLA PFQNTEIYGI LSHILDLPAQ PNNGTYEGAL PLRRNRNSTK EWLLKDIEQA
YSKLI
