FUZ7_USTMA
ID FUZ7_USTMA Reviewed; 435 AA.
AC Q99078; A0A0D1E2E5; Q4PEE9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Dual specificity protein kinase FUZ7;
DE EC=2.7.12.2;
GN Name=FUZ7; ORFNames=UMAG_01514;
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 [GENOMIC DNA].
RC STRAIN=FBD12;
RX PubMed=7926737; DOI=10.1101/gad.8.12.1367;
RA Banuett F., Herskowitz I.;
RT "Identification of fuz7, a Ustilago maydis MEK/MAPKK homolog required for
RT a-locus-dependent and -independent steps in the fungal life cycle.";
RL Genes Dev. 8:1367-1378(1994).
RN [2]
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 [3]
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.
CC -!- FUNCTION: Protein kinase that is necessary for a-locus-dependent
CC processes, such as conjugation tube formation, filament formation, and
CC maintenance of filamentous growth, and for a-locus-independent
CC processes, such as tumor induction and teliospore germination.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U07801; AAA62242.1; -; Genomic_DNA.
DR EMBL; CM003142; KIS70344.1; -; Genomic_DNA.
DR RefSeq; XP_011387552.1; XM_011389250.1.
DR AlphaFoldDB; Q99078; -.
DR SMR; Q99078; -.
DR STRING; 5270.UM01514P0; -.
DR EnsemblFungi; KIS70344; KIS70344; UMAG_01514.
DR GeneID; 23562500; -.
DR KEGG; uma:UMAG_01514; -.
DR VEuPathDB; FungiDB:UMAG_01514; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q99078; -.
DR OMA; EAWASTF; -.
DR OrthoDB; 688282at2759; -.
DR BRENDA; 2.7.12.2; 6587.
DR PHI-base; PHI:2224; -.
DR PHI-base; PHI:402; -.
DR PHI-base; PHI:6068; -.
DR Proteomes; UP000000561; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..435
FT /note="Dual specificity protein kinase FUZ7"
FT /id="PRO_0000085955"
FT DOMAIN 109..417
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 115..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 296..297
FT /note="EL -> DV (in Ref. 1; AAA62242)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="S -> T (in Ref. 1; AAA62242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47201 MW; 7DC3685407E2BBF7 CRC64;
MLSSGAGSSI RKKRNFKGLQ LAESPLASPV DASATTPSHK PGEGSAASNA STIGKSSAVT
PGGSLALPVK NGLDTEPNSG ANYHNKLTQQ LANLELGVEY KLDLKNEDLK TLSELGAGNG
GTVTKVLHEK SGTVMAKKVV FIDAKPSVRK QILRELQILH ECNSPYIVSF YGAYLNEPHI
CMCMEFMQKD SLDGIYKKYG PISPEICGKI AVAVSHGLTY LYDVHRIIHR DVKPSNILVN
GAGQIKICDF GVSGELINSI ADTFVGTSTY MSPERIQGDQ YSVKSDVWSL GVSIIELALG
RFPFAENEED DDSDADNNYT NEDLAGTLSP TKPAPMISLG QNEKQRRRKS KPAGVSLEGS
SHQMSILDLL QHIVNEPPPK LPEGRFPKHM EEFVNLCLLK DPAKRPTPKD LTKHQYVIDA
DAAKVDLQAW ADGMK
