ID A0A0D1BUF3_USTMA Unreviewed; 1079 AA.
AC A0A0D1BUF3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=K, P-type ATPase {ECO:0000313|EMBL:KIS65732.1};
GN ORFNames=UMAG_06433 {ECO:0000313|EMBL:KIS65732.1};
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 {ECO:0000313|EMBL:KIS65732.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS65732.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., 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] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003162; KIS65732.1; -; Genomic_DNA.
DR RefSeq; XP_011392714.1; XM_011394412.1.
DR AlphaFoldDB; A0A0D1BUF3; -.
DR SMR; A0A0D1BUF3; -.
DR EnsemblFungi; KIS65732; KIS65732; UMAG_06433.
DR GeneID; 23566028; -.
DR KEGG; uma:UMAG_06433; -.
DR VEuPathDB; FungiDB:UMAG_06433; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; A0A0D1BUF3; -.
DR OMA; FQDWSTK; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..161
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 119555 MW; 190F0DAA78049363 CRC64;
MSDSKSVSDC DVEKDQIRQT LSDQSHVDTV GPSAAPRVSI KVPRTQTTRS HIPIGFRTLS
IQVYDSRGVE GAKSNDHLSD SDFFGSLDFH TVDPDALAQR FNVLPESGLD TPAATRRLER
NGKNVLTQKK NKYWLKLFHY TFGGFCSILW IGVIIFFISW RPLGNPPQAY NLALAIVVLI
VIFFQAIFNA FQDWSTQKVM NSILHLLPEN AVVIRDGEHK SISASELVVG DVCILSTGNK
VPADMRIIKA SADLKFDRSV LTGESEEIPG TVEPTETNFL ETKNIALLGT HICNGNATGI
VVLTGPRTVM GRINKLTNDD KEKPTQLQKE ISRFVYIIIG LTVTLVLIML ITWLAWLRKD
HPGFLNTVGI LTNLMSLVVA FIPEGMPVAV ALTLSLIARR MRDVRVLPKS LSTVETLGCV
NVICSDKTGT LTENKMSVNS IGFVDKECTR IDISSIDQPA VFDELNKGMA LCNDAFFDPS
SDAVLPSERS VQGNATDAAV LRLSASLPGS EEIKASFRRV YDIPFNSKNK FMLTVMRSNS
DKATTTADEM FVKGAPDVLM PRISHFFSAR DGQTKVFDDM ARSQLVSKQE AWSRRGERVI
LLAKRQFIAS SKPGTGEYED EVAAASQEDL IVIGLLGIMD PPRSDIRHTV AECRRSGSRF
FMVTGDFSLT AAAIGKMVGI FTHNGEPDCI ANFDVKGRYV SEPPALNEKA LKKQNGPKDI
IEASLLVEGK EIPQITQQQW DVVCRYEEIV FARTTPEQKL KIVNELRDRG CVVAVTGDGV
NDAPALKAAD VGIAMVSGSD VAMEAADLVL MGDFSSIIQA IKLGRLVFQN LQKVISYLLP
AGSWSEDWPV ILNVFFGVPL PLSSFLMIII CCFTDLVCCL TLIFEKEEFD LLSLAPRNPR
SDHLVNKAIY GQSYLFIGMM ETLTAHSMFF LYIWKYAKIP VKDMFFAFEK FGDGFHGYTA
DELNHFLAVG QCVYFVTLVI LQWGNLLSVR NKRLSIFQAD PIRKQRRNPY LILGPLAALV
IAIFVTEVKG IQNLFGTASI PIEFWLIPVP LAIGILVMDE LRKLLVRTFP NSIIAKIAW
//
