KHD4_USTMA
ID KHD4_USTMA Reviewed; 1416 AA.
AC A0A0D1DXB8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=K homology domain-containing protein 4 {ECO:0000303|PubMed:15643068};
GN Name=KHD4 {ECO:0000303|PubMed:15643068}; ORFNames=UMAG_03837;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=15643068; DOI=10.1128/ec.4.1.121-133.2005;
RA Becht P., Vollmeister E., Feldbruegge M.;
RT "Role for RNA-binding proteins implicated in pathogenic development of
RT Ustilago maydis.";
RL Eukaryot. Cell 4:121-133(2005).
RN [4]
RP FUNCTION, DOMAIN, RNA-BINDING, AND MUTAGENESIS OF 765-GLY--ASN-768 AND
RP 833-GLY--GLY-836.
RX PubMed=19854870; DOI=10.1261/rna.1817609;
RA Vollmeister E., Haag C., Zarnack K., Baumann S., Koenig J., Mannhaupt G.,
RA Feldbruegge M.;
RT "Tandem KH domains of Khd4 recognize AUACCC and are essential for
RT regulation of morphology as well as pathogenicity in Ustilago maydis.";
RL RNA 15:2206-2218(2009).
CC -!- FUNCTION: RNA-binding protein that recognizes the sequence AUACCC via
CC its tandem KH domains 3 and 4, probably in order to promote mRNA
CC instability (PubMed:19854870). Plays an essential role in filamentous
CC growth and virulence (PubMed:15643068). {ECO:0000269|PubMed:15643068,
CC ECO:0000269|PubMed:19854870}.
CC -!- DOMAIN: The tandem KH domains 3 and 4 are essential for AUACCC binding.
CC {ECO:0000269|PubMed:19854870}.
CC -!- DISRUPTION PHENOTYPE: Affects cell growth, pheromone response,
CC filamentation, cell morphology, as well as pathogenicity
CC (PubMed:15643068). Leads to increased levels of mRNAs containing the
CC AUACCC sequence (PubMed:19854870). {ECO:0000269|PubMed:15643068,
CC ECO:0000269|PubMed:19854870}.
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DR EMBL; CM003149; KIS68256.1; -; Genomic_DNA.
DR RefSeq; XP_011390271.1; XM_011391969.1.
DR STRING; 5270.UM03837P0; -.
DR EnsemblFungi; KIS68256; KIS68256; UMAG_03837.
DR GeneID; 23564186; -.
DR KEGG; uma:UMAG_03837; -.
DR VEuPathDB; FungiDB:UMAG_03837; -.
DR eggNOG; KOG2208; Eukaryota.
DR OMA; FNFEVRF; -.
DR OrthoDB; 753986at2759; -.
DR Proteomes; UP000000561; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 2.
DR SMART; SM00322; KH; 5.
DR SUPFAM; SSF54791; SSF54791; 4.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; RNA-binding; Virulence.
FT CHAIN 1..1416
FT /note="K homology domain-containing protein 4"
FT /id="PRO_0000454344"
FT DOMAIN 412..504
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 508..594
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 747..816
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 817..892
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 900..968
FT /note="KH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 25..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 765..768
FT /note="GKKN->AAAA: Completely abolishes mRNA-binding."
FT /evidence="ECO:0000269|PubMed:19854870"
FT MUTAGEN 833..836
FT /note="GVGG->AAAA: Completely abolishes mRNA-binding."
FT /evidence="ECO:0000269|PubMed:19854870"
SQ SEQUENCE 1416 AA; 151429 MW; 23C780E5D1FDDFBC CRC64;
MDFYSTSFTI PRSIGASSFV TETTNPNGSI TAASSSSFSL EAPRPGSHVG ARTAPTASAA
PEPPASSLPG RFTSMRSRFP PSVKAFMPSA FGGKRTSDRI VEAVGAEKAE ADAATGSSSQ
PVKAEPEQSA PLAPIGERGN ARPSKLVNPS LANMDDNGSS QHRDSRSTVG TRSSFDISSA
ASFTADSTAA SSAIGVNSSS TTHSASNSIS ANHVQQDRGI SLSQSSKDLQ EAIQKLSSDI
MANHQCLVSF ASVPQNDESR MPPTPLSHPF ARQSSFSSLQ SLDQLPFPNP NGSSGYPYQQ
YHPQPIGTPD SHSSAFFPGR AAGEALGSGF PGLNSSSLSL SSLNPPASGS HVAQEVGLSS
AQPLRSPQPN AIGASRASLS SMPKPPQYNF HLSGGYQQVM NARGTILREN PFKSTSSIKV
PRADVFDVAP ASSPPAKESI KEDVRRKLDE VQTATGATIT LKNSEVRGAD LGYGLETERI
VEVLVSGTFE SVELARVKVL VILDEIAGLR SETCEIDYKL HNIIGGRKRC VVQKIEEETG
TSIYLPSSFL GTFGSSLASR NDGKAVAAHQ NQIHITGEFF GVQRARDMLF QVSMHKSKGI
ISRDAAILPR KLDWMLTDRL EELRSIMIDN GTFVAFPLLG SQTSVISVFG DHRVNIERTI
RSIMQLACQF YVASLWLLPV GFDVYMPSPQ ANLNPTQVAP MLKHVANASG AEVVFKSNCF
EIHGLESEVR TAVSALLELE LIKSFNFEVR FQIELANEHR EFISGKKNGK VNKVMKQCGV
RIKFETFNDY NFLIDVSGND RNGVLQGLGL LQEELPAEMS FHVPEAYHKR IIGVGGKNIQ
RIMKKFGVYV KFSNAEEFAA LGGYLDNEDN VIARTPAKNA ANLENLKLSV MELVNPKDKD
YISETVTISR RYHRTLLGEK AIFIHDIESK TSSSVRFPAR ESASDLVTIF GPESQIHIAA
QMLLDHVPFE AEFRAPNSTE LGDAIHSAEF AALAEQLKRD LSISVSPVIE QRRPGGEAVF
KLRLNRSNTD FLPTAKDAIE DFLINRNANI YAAPSRTRSD SFASAFPHFA NKLISTAGAA
ESNESFNTAA AAAAAAAEQA RVNERRLRAA ASTPDIKALF DAPSQHLHGG PGFASSNGGS
AATAANSPLI TSPLYTSPYG NGRGFGSDVW GAPTRAFTAS NASNATPSLM GLPPPSVGTP
GAGLVSAAGP GPIGAGVSVP TSGGIQFPSQ PSLHQQSGHR LSDEMHMNRG LEGMSMEDRV
KALRKPRSFA HRAQSLDIGA MAAQQASQHA SGSMSVGPST PYGLGPIGTG APGMSGHFPG
MTSSQGTFGG GAPHHLYQPP TPQQQAQQQL QYQQQQQQQQ QQQQQPGYGM PHQPQHFHAS
SASISRLPPG RNTQNPDSTT MDEVSRVLAQ LAFDRA
