ID A0A4Y9YKQ9_9APHY Unreviewed; 1504 AA.
AC A0A4Y9YKQ9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=EVJ58_g3509 {ECO:0000313|EMBL:TFY62995.1};
OS Rhodofomes roseus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Rhodofomes.
OX NCBI_TaxID=34475 {ECO:0000313|EMBL:TFY62995.1, ECO:0000313|Proteomes:UP000298390};
RN [1] {ECO:0000313|EMBL:TFY62995.1, ECO:0000313|Proteomes:UP000298390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105464 {ECO:0000313|EMBL:TFY62995.1,
RC ECO:0000313|Proteomes:UP000298390};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Fomitopsis rosea.";
RL Submitted (JAN-2019) 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:TFY62995.1}.
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DR EMBL; SEKV01000145; TFY62995.1; -; Genomic_DNA.
DR STRING; 34475.A0A4Y9YKQ9; -.
DR Proteomes; UP000298390; 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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 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|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW 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:UP000298390};
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 636..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 673..691
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1239..1261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1308..1332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1344..1362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 350..458
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1504 AA; 161837 MW; C85C48FC28A492C8 CRC64;
MSQPDSSRPE IPSIVTTDLS SNTNLSSGVD DQHVELDVQP PTPTGQQFLS ASPTYLSPSG
RRPSVTGQSS LDAPYSPTAT VSPTLGQRSP SPSYAGSISG SSQHVPPSPT LSAHSSVHFA
SSLALRDNKP EQRDGISSLG LLTPNAGYKH RRKGSVASSV GSDGTEPDVQ LSEYGMVSVI
SPRHDDEYKS ASIPPSPTHT HFDGASVNGA ASEFDGTTMR SRSGSAHSRA KLISPQPPDD
QDPKASSKKG KNVNGGDGED QPDDKDSPRP ALDLSADDAL DAGPFAFKPF RLASLVDPKS
LSSLEQMGGI EGLLGGLGTH AKQGLSAVAI TEATDSKPVM GAGESEGAGQ RHDRPQEESA
RSQSGETEEE VVPGIVVTGP GSEVDVTRKS NLADSQSDDE VGEKAYDASM DERRRVFGAN
VLPTRKTKSL LQLMWLALKD KVLVLLSIAA VVSLALGFFQ DFGTPRPAGE PPVDWSKVLV
GSVNDWQKER QFQTLNEKKE ERGVKVIRAG NERVVDVHEV VVGDVAILEP GEIIPCDGVF
LGGHNVRCDE SGATGESDAI RKIDYEEALR ARDGHSEHGS HADCFMVSGS KVLEGYGSYV
VIAVGPKSFN GRIMMALRGD TEDTPLQLKL NDLAELIAKA GSIAGLALFV ALMIRFFVQL
GTNDPARTAN QKGIAFVNIL IISVTLIVVA VPEEYEGLPL AVTLALAFAT KRMTKENLLV
RVLGSCETMA NASVVCTDKT GTLTQNSMTI VAGTVGIHCK FVRNLSDNRS RTNAEGDQQT
QDRQAEDVLQ GARPTNGKRK HSQDFSIDQS EMNRFLHPAL RELFNEAIAI NSTAFEDTDP
DTNELVFIGS KTEMALLKFA KELGWADYKK TREAADIVQM IPFSSSRKAM GVVVKLGDGR
CRLYLKGASE ILARKCTSYV TVTRGGDASE SAGVETREID DLARDNVSRT IIFYANQTLR
AITLCYRDFE SWPPAGASYT ADDEVEYEDL ARDLTLIAIT GIEDPLREGV REAVADCFKA
GVTVKMCTGD NVLTARSIAL QCGIFSEGGL IMEGPVFRKL NDQELLEAVP RLQVLARSSP
EDKKLLVEKL RELGEIVGVT GDGTNDGPAL KTADVGFSMG IAGTEVAKEA SDIILMDDNF
ASIVKAIMWG RCVNDAVRKF LQFQLSTNVT AVVVTFVSAV ASASESSVLS AVQLLWINII
MDTFAALALA TDPASPALLD RKPEGKTAPL FSVNMYKQII GQSAYQILIV LLFHFLGAQI
LGFDPKYSST VSQTTVFNIF VFAQITNSVN CRRLDNRLNI FEGITRNYYF MVVTLIEVAV
QILIVFVGGA AFSVTRIGGA EWGISLALGL VSIPLGALIR CIPNEPVERL LKALHIMSNP
AVLPTTRTDG DWNTAIELVR DNLNTFAHVR GGRMRASSYV DRSRKARPLP ETELGLPSIM
TMVPTLIASS IGRAPLSPNG LADPTQFDPS KSSAALWEGR IQVHPDTKPD DPTRQRWENE
PSPC
//
