SMH1_MAIZE
ID SMH1_MAIZE Reviewed; 299 AA.
AC Q6WS85; B6TMI8; Q6VSV4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Single myb histone 1;
DE AltName: Full=Protein SINGLE MYB HISTONE1;
GN Name=SMH1; ORFNames=ZEAMMB73_836537;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. B73, and cv. Missouri 17; TISSUE=Mesocotyl;
RX PubMed=14576282; DOI=10.1104/pp.103.026856;
RA Marian C.O., Bordoli S.J., Goltz M., Santarella R.A., Jackson L.P.,
RA Danilevskaya O., Beckstette M., Meeley R., Bass H.W.;
RT "The maize Single myb histone 1 gene, Smh1, belongs to a novel gene family
RT and encodes a protein that binds telomere DNA repeats in vitro.";
RL Plant Physiol. 133:1336-1350(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- FUNCTION: Binds preferentially double-stranded telomeric repeats 5'-
CC TTTAGGG-3', but can also bind to the single G-rich and C-rich telomeric
CC strand. {ECO:0000269|PubMed:14576282}.
CC -!- SUBUNIT: Forms a homodimer and heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-
CC ProRule:PRU00837}. Nucleus, nucleolus {ECO:0000250}. Chromosome,
CC telomere {ECO:0000305}. Note=Localized to the nucleolus during
CC interphase. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:14576282}.
CC -!- DOMAIN: HTH myb-type domain confers double-stranded telomeric DNA-
CC binding while the H15 domain is involved in non-specific DNA-protein
CC interaction and multimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. SMH subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00837}.
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DR EMBL; AY271659; AAQ01754.1; -; mRNA.
DR EMBL; AY328854; AAR01211.1; -; Genomic_DNA.
DR EMBL; CM000784; AFW83118.1; -; Genomic_DNA.
DR EMBL; EU966203; ACG38321.1; -; mRNA.
DR EMBL; BT042177; ACF87182.1; -; mRNA.
DR RefSeq; NP_001141858.1; NM_001148386.1.
DR AlphaFoldDB; Q6WS85; -.
DR SMR; Q6WS85; -.
DR STRING; 4577.GRMZM2G136887_P02; -.
DR PaxDb; Q6WS85; -.
DR PRIDE; Q6WS85; -.
DR EnsemblPlants; Zm00001eb357490_T003; Zm00001eb357490_P003; Zm00001eb357490.
DR GeneID; 100274000; -.
DR Gramene; Zm00001eb357490_T003; Zm00001eb357490_P003; Zm00001eb357490.
DR KEGG; zma:100274000; -.
DR MaizeGDB; 894674; -.
DR eggNOG; ENOG502QSU2; Eukaryota.
DR HOGENOM; CLU_047477_0_1_1; -.
DR OMA; DMKLAHG; -.
DR OrthoDB; 1114012at2759; -.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; Q6WS85; baseline and differential.
DR Genevisible; Q6WS85; ZM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR044597; SMH1-6.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46267; PTHR46267; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Telomere; Transcription; Transcription regulation.
FT CHAIN 1..299
FT /note="Single myb histone 1"
FT /id="PRO_0000429013"
FT DOMAIN 1..61
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 124..192
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DNA_BIND 28..57
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT COILED 238..279
FT /evidence="ECO:0000255"
FT CONFLICT 6
FT /note="Q -> H (in Ref. 3; ACG38321)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="D -> N (in Ref. 3; ACG38321)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="P -> S (in Ref. 3; ACG38321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 32576 MW; B41E902F9F32EBBD CRC64;
MGAPKQRWTP EEEAALKAGV AKHGPGKWRT ILRDSDFSAL LRLRSNVDLK DKWRNLSVTA
GGYGSREKAR MALKKGRRVV PKLTAEPMDV DVKDMDDAHD TAIDVEPLAM AFESLPTEES
PDKSVARLDD LILEAIRKLK EPSGPSKAAI AAYIEDQYWP PADFQRLLST KLKALVNSGK
LIKVNQKYRI APSPPPSGRI GTKVSSAEGM KAENNNAKRL TKHQVIAELE KMKGMTKEEA
AAFAAKAVAE AEVAIAEAEE AARVAEAAEN DAEAAKAFLD AVTLSMRNRN AASMMLRAC
