ID A0A4U0V2Z2_9PEZI Unreviewed; 1418 AA.
AC A0A4U0V2Z2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=B0A54_06969 {ECO:0000313|EMBL:TKA42753.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA42753.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA42753.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA42753.1,
RC ECO:0000313|Proteomes:UP000310066};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:TKA42753.1}.
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DR EMBL; NAJP01000021; TKA42753.1; -; Genomic_DNA.
DR STRING; 329885.A0A4U0V2Z2; -.
DR Proteomes; UP000310066; 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; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 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; 2.
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; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000310066};
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 269..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 301..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 469..487
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 507..537
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 956..977
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 989..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1103..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1138..1156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1298..1318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 237..280
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 983..1156
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 153131 MW; B6674EAECE1EB277 CRC64;
MDQELDRLSD DGRSTKGDRS PTGLQPGSRS LLTPTKLRAS NSFDSRDSRP TSLHNVSSPP
QWSNPHNFLA VPPTQRSRGQ SFDTEASQES ASDITYVNTN TPSSDNTPNA FASHDKEVGA
GNHQVLPDNE ALRPDKGTEE DFNRPNNPFA FAPGHMTKML NPKSLGAFHA VGGIAGLEKG
LRTDRDAGLG GDENRLAGSV SFEEATASTS PASDITVVES PEIAPQLSGS KAHTGNFEDR
KRIFSDNRLP ERKAKSIFQL MWLAYNDKVL IVLSVAAVIA LALGLYQALG TKAGGVDWIE
GVAIMVAIIV VVVVGALNDW QKEKQFAKLN KKKDDRNVKL IRSGRTQEIS IHDVLVGDVL
LVEPGDILPV DGLFIAGHSV KCDESSATGE SDITKKTPAE EVFRVMEAGE PLKKMDPFMI
SGGKVTEGVG RMLVTATGVH SSYGKTMMSL QDSTEATPLQ TKLNGLAEYI AKIGSAAALL
LFTVLLIKFC AQLPHDKRAP ADKGQAFMTI LITAVTIIVV AVPEGLPLAV TLALAYATKR
MLKDRNLVRV LRSCETMGNA TTVCSDKTGT LTQNVMTVVA GSVGTSNRFS SRAGSNGDAA
ADVDTVGVTT TEFISSLDHN VKTLWKDSIA VNSTAFEGDA EGRKVFIGSK TETALLDFAR
DNLGMDSVSV ERSNSEIVQM IPFDSSRKCM GMVVKLRDRK GYRLLVKGAS EIMLRFCSSI
SCDPRKGLEQ ATMTGDDRKT LQALIDAYAD KTLRTIGFIY RDFESWPPRN CRRQEDDRTQ
AVFEDICKDM TFFALVGIQD PLRPGVAEAV KDCIMAGVYP RMVTGDNILT AKAIARECGI
YTAEGVALEG PEFRKMSHAD QRAIIPKLQV LARSSPEDKR MLVKRLKEMG ETVAVTGDGT
NDAPALRAAD VGFSMNISGT EVAKEASDII LMDDNFASIV LALMWGRAVN DAVRKFLQFQ
ITVNITAVLL AFISAVASAE EQSVLTAVQL LWVNLIMDTM AALALATDPP SRQILDRKPD
PKSAPLISPT MWKMVLGQAI YQLTITLVLN FAGNQILGYT TPIQQREKQT LVFNTFVWMQ
IFNALNNRRL DNRFNVFEGL TKNLFFCAIF LVMIAGQILI VFVGGWPAFQ AQRQNGTQWA
IALVLGFLSL PIGVLIRCIP DELATRAVPG PIRRWVSRDK SAKNKIVVTD EEAAVAPSGG
LEYNQALYGI QQELAWIRKY RGGRLNALKF AVKHPREALA RSRSPSLRSR SRASSSLPRT
PNNEVVVVDD VDGAGQSPVG PPTPDSRRSR RGRRRSENSA FAATAMAGIV AGSIAGGWSP
IERAPGDGES VRFGRDRSKS DLSSREIPRE GVPPLETGVR TGTGTGMGGL LVVPGGGPGE
GSRNLLPPGR VPAGAAPEVG GGLFGGRLGE QTERKKGG
//
