ID   MLO2_SCHPO              Reviewed;         329 AA.
AC   Q09329;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Protein mlo2;
GN   Name=mlo2; ORFNames=SPBC4.05;
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 [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8972853; DOI=10.1093/nar/24.23.4676;
RA   Javerzat J.-P., Cranston G., Allshire R.C.;
RT   "Fission yeast genes which disrupt mitotic chromosome segregation when
RT   overexpressed.";
RL   Nucleic Acids Res. 24:4676-4683(1996).
RN   [2]
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   -!- FUNCTION: Not known, interfere with mitotic chromosome segregation when
CC       overexpressed.
CC   -!- SIMILARITY: Belongs to the UBR7 family. {ECO:0000305}.
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DR   EMBL; L42550; AAB41271.1; -; mRNA.
DR   EMBL; CU329671; CAB58404.1; -; Genomic_DNA.
DR   PIR; T40419; T40419.
DR   RefSeq; NP_595478.1; NM_001021389.2.
DR   AlphaFoldDB; Q09329; -.
DR   BioGRID; 277126; 16.
DR   STRING; 4896.SPBC4.05.1; -.
DR   iPTMnet; Q09329; -.
DR   MaxQB; Q09329; -.
DR   PaxDb; Q09329; -.
DR   PRIDE; Q09329; -.
DR   EnsemblFungi; SPBC4.05.1; SPBC4.05.1:pep; SPBC4.05.
DR   GeneID; 2540600; -.
DR   KEGG; spo:SPBC4.05; -.
DR   PomBase; SPBC4.05; mlo2.
DR   VEuPathDB; FungiDB:SPBC4.05; -.
DR   eggNOG; KOG2752; Eukaryota.
DR   HOGENOM; CLU_025221_1_0_1; -.
DR   InParanoid; Q09329; -.
DR   OMA; ECNEDWY; -.
DR   PhylomeDB; Q09329; -.
DR   PRO; PR:Q09329; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR040204; UBR7.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR13513; PTHR13513; 2.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..329
FT                   /note="Protein mlo2"
FT                   /id="PRO_0000096500"
FT   ZN_FING         33..104
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT   ZN_FING         120..179
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
SQ   SEQUENCE   329 AA;  38079 MW;  4254A4382917195F CRC64;
     MEETAHELTV KQYVEQQREL EREAREVLPY SFDTCTYSMG YLKQPLYACL TCQKASGSLN
     AVCYSCSISC HADHDLVDLF NKRHFRCDCG TTRTHSIPCN LRKSVDECGS ENDYNHNFEG
     RFCICDTVYN PETEEGTMFQ CILCEDWFHE KCLQKTNKGI AIPDAETFEW LVCSECSEKY
     RDHLLNQKHE SIAGTERAPL FLSENFRENL CPCESCISLR NLEMPMLVAE EPIYEPPEDS
     EDGISEMNED PSESGEMIEQ VISSTMNDVL RILDRLPRVQ ANESVYAYNR LKSELTDFLT
     PFARENRVVT KEDISNFFLE RSRISKNLR