SMH3_MAIZE
ID SMH3_MAIZE Reviewed; 285 AA.
AC Q6WLH4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Single myb histone 3;
DE AltName: Full=Protein SINGLE MYB HISTONE3;
GN Name=SMH3; ORFNames=ZEAMMB73_537819;
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 [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC TISSUE=Leaf;
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 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 [3]
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).
RN [4]
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).
CC -!- FUNCTION: Binds preferentially double-stranded telomeric repeats, but
CC may also bind to the single telomeric strand. {ECO:0000250}.
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 -!- 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; AY280629; AAQ62066.1; -; mRNA.
DR EMBL; CM000784; AFW83707.1; -; Genomic_DNA.
DR EMBL; EU962838; ACG34956.1; -; mRNA.
DR EMBL; BT053836; ACL52443.1; -; mRNA.
DR RefSeq; NP_001105225.1; NM_001111755.1.
DR AlphaFoldDB; Q6WLH4; -.
DR SMR; Q6WLH4; -.
DR EnsemblPlants; Zm00001eb361200_T001; Zm00001eb361200_P001; Zm00001eb361200.
DR GeneID; 542123; -.
DR Gramene; Zm00001eb361200_T001; Zm00001eb361200_P001; Zm00001eb361200.
DR KEGG; zma:542123; -.
DR HOGENOM; CLU_047477_1_0_1; -.
DR OMA; KWKNIIR; -.
DR OrthoDB; 1011236at2759; -.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; Q6WLH4; baseline and differential.
DR Genevisible; Q6WLH4; 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; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS: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..285
FT /note="Single myb histone 3"
FT /id="PRO_0000429015"
FT DOMAIN 1..60
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 113..181
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DNA_BIND 28..56
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..255
FT /evidence="ECO:0000255"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 31347 MW; A78841D5C7DC4FC8 CRC64;
MGAPKQKWTS EEEDALRRGV RKHGAGKWRT IQKDPQFSPI LSSRSNIDLK DKWRNLSFSA
SGLGSSKVRV PKITGSSSSP SSSSQALLLP AANNVTEAML PADADKKPRD GKTPPKYGAM
IMEALSELNQ PNGSDIDAIF DFIKQRHVVQ STFRRFLPSK LRRLADSNKI EKVDNFYRLP
DSFATRTPAQ IKVSDPKQKD PSKASKTIGL FAASSPALEA AMAAAVKVTD AEAKAHDAHD
QMMEAERMLK MAEDTESILT IAAEIYDRCS RGEITTLVPV AQREF
