ID A0A066VU20_TILAU Unreviewed; 1001 AA.
AC A0A066VU20;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=K437DRAFT_256669 {ECO:0000313|EMBL:KDN45222.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN45222.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN45222.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN45222.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN45222.1}.
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DR EMBL; JMSN01000044; KDN45222.1; -; Genomic_DNA.
DR RefSeq; XP_013243079.1; XM_013387625.1.
DR AlphaFoldDB; A0A066VU20; -.
DR STRING; 1037660.A0A066VU20; -.
DR GeneID; 25264490; -.
DR HOGENOM; CLU_002360_3_2_1; -.
DR InParanoid; A0A066VU20; -.
DR OMA; PLWNNMM; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000027361; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR CDD; cd02083; P-type_ATPase_SERCA; 1.
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; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000027361};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 290..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 757..778
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 790..809
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 830..852
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1001 AA; 108691 MW; 9165D0D9C5D055DD CRC64;
MDAAWTHTVE ECIKALGSDA KKGLSSSEIA ERHTKYGKNA LPEQAGDSLF KLILDQFKDQ
LVLILLASAV ISFVLALLEE YESLGTALIE PGVIFLILIA NATVGVVQER NAEESIEALK
KYSPDNASVV RDGSTLRVKA EELVPGDILV IAVGDKVPAD CRLIAINSSS FRVDQAILTG
ESIAVNKDLS PVADARAVKQ DMTNTLFSGT TIVSGSGVAI VVRTGEKTAI GDIHAEISQK
DADEKTPLKQ KLDEFGDMLA KVISVICILV WLVNIRHFSD ASHHGTLKGA IYYFKIAVAL
AVAAIPEGLA AVITACLALG TKKMAAKNAI VRHLPSVETL GSTNVICSDK TGTLTTNQMS
VTRFLVFGDS AADVREFDVE GSSYAPEGAI TSTAASNPVG KLNVADSSIQ ALAEVAAVCN
DAQVVYSAED KRYNCIGQPT EAALKVLVEK IGHHDNTANA SFATLDAVQR ANAVSTLYQA
SIPRLLTLEF SRDRKSMSVL IRRTDNSGVL LVKGAPETVL DRCSFLHLGK ARAQMTPAIR
NSLNDKVADY ATRGLRCLVL AVAEGVPLDI QAYKSETTAE YARYEQNMTF VGLVGMLDPP
RPEVRGAIER CRSAGIRVIV ITGDNKNTAE TICRQIGVFG DSEDLTGKSY TGREFDELDD
QAKRDAVLRA SLFSRTEPTH KSQLVDLLQE QGLVVAMTGD GVNDAPALKK ADIGIAMGTG
TDVAKSAADM VLADDNFATI ETAVEEGRSI YNNMQSFIRY LISSNIGEVV SIFLTVLLGM
PEALIPVQLL WVNLVTDGLP ATALGFNPPD HEVMRHKPRR REDPLVSKWL FIRYLLIGTY
VGVATVGGYA WWFMFYEGGP QISFYQLTHF HQCGTLFPEI GCEMFVNELS KRATTISLSI
LVTIEMFNAL NSLSEEDSLL VQPPTKNPFL IFAIVLSMAL HFMILYTPFL RELFVITPLN
WAEWKGVLYI SAPVILIDEV CKWITRTFVN PPTGVKKLKE A
//
