YLW2_SCHPO
ID YLW2_SCHPO Reviewed; 225 AA.
AC Q9UT12;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Uncharacterized protein P8A3.02c;
GN ORFNames=SPAP8A3.02c;
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] {ECO:0000312|EMBL:CAB55169.1}
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).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000255}.
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DR EMBL; CU329670; CAB55169.1; -; Genomic_DNA.
DR PIR; T39239; T39239.
DR RefSeq; NP_594941.1; NM_001020372.2.
DR PDB; 5YL6; X-ray; 2.00 A; A=36-219.
DR PDB; 5YLB; X-ray; 1.79 A; A=33-219.
DR PDBsum; 5YL6; -.
DR PDBsum; 5YLB; -.
DR AlphaFoldDB; Q9UT12; -.
DR SMR; Q9UT12; -.
DR BioGRID; 277997; 8.
DR STRING; 4896.SPAP8A3.02c.1; -.
DR MaxQB; Q9UT12; -.
DR PaxDb; Q9UT12; -.
DR EnsemblFungi; SPAP8A3.02c.1; SPAP8A3.02c.1:pep; SPAP8A3.02c.
DR GeneID; 2541495; -.
DR KEGG; spo:SPAP8A3.02c; -.
DR PomBase; SPAP8A3.02c; -.
DR VEuPathDB; FungiDB:SPAP8A3.02c; -.
DR eggNOG; KOG4176; Eukaryota.
DR HOGENOM; CLU_1107658_0_0_1; -.
DR InParanoid; Q9UT12; -.
DR OMA; WLHEIPF; -.
DR PhylomeDB; Q9UT12; -.
DR PRO; PR:Q9UT12; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:PomBase.
DR GO; GO:0008198; F:ferrous iron binding; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; IDA:PomBase.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:PomBase.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Nucleus; Oxidoreductase; Reference proteome;
KW Vitamin C.
FT CHAIN 1..225
FT /note="Uncharacterized protein P8A3.02c"
FT /id="PRO_0000315939"
FT DOMAIN 114..219
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:5YLB"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5YLB"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5YLB"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5YLB"
SQ SEQUENCE 225 AA; 25991 MW; 4B7CD0194371174F CRC64;
MLYENMSDSF LLSDAGLEFD EALLEVDQEK DDYLDDFENW TVVPVETIEG INYYPNCLPE
SVQRNLINNV PKELLSIYGS GKQSHLYIPF PAHINCLNDY IPSDFKQRLW KGQDAEAIIM
QVYNPGDGII PHKDLEMFGD GVAIFSFLSN TTMIFTHPEL KLKSKIRLEK GSLLLMSGTA
RYDWFHEIPF RAGDWVMNDG EEKWVSRSQR LSVTMRRIIE NHVFG
