ID A0A317XNQ6_9BASI Unreviewed; 1036 AA.
AC A0A317XNQ6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=BCV70DRAFT_200120 {ECO:0000313|EMBL:PWY99944.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY99944.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWY99944.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY99944.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819193; PWY99944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XNQ6; -.
DR STRING; 1882483.A0A317XNQ6; -.
DR InParanoid; A0A317XNQ6; -.
DR Proteomes; UP000246740; 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 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; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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:UP000246740};
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 386..404
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 416..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 887..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 933..950
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 962..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 992..1010
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 110..186
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 111091 MW; D5B80B06F5FB5B82 CRC64;
MAFDSRYRPV PTGDYDVSAV GPSALPTQLP SSDQFAFSTT LRKANTDEPY GVQPSSSYPP
TSPPRAGHKP KFSDSSYRGD LHSLDLDPSS AGPSRRTAAA SASRSSASVR FTHLSVSDTL
AALHCPSLER GLTPLQVHEA RREAGGYNEF AVRGGEEPWR KFLGQFQEPL ILLLLGSAGV
SLLTGQIDDA VSITIAIIIV ISVGFYQEQK SEKSLEALNK LVPHYCHLVR EGVTSNVLAN
ELVPGDVVTF STGDRVPADI RICSSVSLEI DESTLTGEIK PRKKHSDVVP HSHHASNGLN
GVNGHAGNAP NGNGDSAHND DQHVTSINER ENIAFMGTLV KSGHGKGVVI GTGAATEFGM
IFSMVDEVAE KRTPLQLNMD ELAKKLSVVS FAVIAVICLM GVWQRRPWLE MFTIGVSLAV
AAIPEGLPIV VTVTLALGVL RMSNRKAIVK KLPSVETLGS VSVICSDKTG TLTSNEMTVV
KCYTAEDGIL DLTQALPHTQ NRALSRTLLV GNLCNNSHRN EQGTNVGQAT DVAMVNVLRL
FGSEDKRPYF RRSSEVAFDS ETKFMAVTGT LSTANPATET TYMKGALEVV LERCSNILGP
DGSPIRLDDA WMKKVTEAAH GLSGEGLRVL ATASGPAGAL DSKTMTFAGL QAMQDPPRPG
VKEAIAALAK GGVQVIMITG DAESTATAMA RQLGILTNSG SSSVMTGRQL DSLTERQLQE
RIGSVSVFAR TTPRHKMSII SAFQSNGAVV AMTGDGVNDA PALKMADIGI SMGKGGTDVA
KEAADVILVD DNFATILSAV EEGKGIFYNI QNFLSFQLST AVAALTLITL STAFRLKLPL
NAMQILFINI LMDGPPSQSL GVDPVDRKSV MSRPPRAKNA PVLNSRLIKR ILFSATMVVL
GTLYIYIHEL VPVDIEVDPE AQPGRFADQR DSTMTFTCFV FLDLVSAVQN RGLYTPLTAN
RMLGLTVGIS FFAQLAMVYF PLLQGVFQTT ALAFQDLLLL AFIAAISFAA HEARRLYERR
LADDEVQELE ARSSWA
//
