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Database: UniProt
Entry: A0A1E3PJ55_9ASCO
LinkDB: A0A1E3PJ55_9ASCO
Original site: A0A1E3PJ55_9ASCO 
ID   A0A1E3PJ55_9ASCO        Unreviewed;      1185 AA.
AC   A0A1E3PJ55;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=NADFUDRAFT_47104 {ECO:0000313|EMBL:ODQ65451.1};
OS   Nadsonia fulvescens var. elongata DSM 6958.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX   NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ65451.1, ECO:0000313|Proteomes:UP000095009};
RN   [1] {ECO:0000313|EMBL:ODQ65451.1, ECO:0000313|Proteomes:UP000095009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ65451.1,
RC   ECO:0000313|Proteomes:UP000095009};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454410; ODQ65451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3PJ55; -.
DR   STRING; 857566.A0A1E3PJ55; -.
DR   OrthoDB; 847at2759; -.
DR   Proteomes; UP000095009; 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; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000095009};
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        156..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        409..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        862..883
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        889..911
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        932..956
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        976..992
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1012..1036
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1042..1061
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          85..172
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  130217 MW;  5BD9C7F19EF860FC CRC64;
     MPSSSPSNIG NSPFSSRSNS RSSSSLLHSE QADASSAAAK KSSKPITSTR QGRTSTLQNN
     NIHRNDNDIY TISPEQLSKL CDTKDFGQLS AFGGFNALVR DLDTDINAGL SADELANSLS
     SGSSNSRVKV YGRNVLPVKR ANSILKLMWI ALNDQVLILL SVAAVISLAL GLYQTFTQPP
     DHDSQGNVLP RVDWIEGVAI VVAIGIVVIV GAINDWQKER QFIKLNEKKE DRKIKAIRSG
     KTQEISIYDI LVGDIVLLEP GDMVPADGLL ISGYNVTCDE SSATGESDTI KKVLVNDCEQ
     RMQSSDAETV NPPDCFIISG SKILEGAGHY LITAVGVNSR YGHTMASLQT ETEETPLQVK
     LDGIANGIAK LGSLAALVLF TVLLIKFLVN LPHYTEIGLT PAQKGQKFIK ILITAITVVV
     VAVPEGLPLA VTLALAFATS RMLKDNNLVR LLKACETMGG ATTVCSDKTG TLTQNKMTVV
     MGTLGLDSEF KVNMDDMAPG DNTSLSSHHL YDHSVKNWFN SSLSDSSRQL LFDSIIINSS
     AFEVEEASNN LKAENFIGSK TETALLNFAK YYLDLKDLAQ KRACYEIVQL YPFDSGRKCM
     LTIIKLQKSR PELKEKESYR VFIKGAAEVL LKKCSRYYDT KADRGHNMCP NDFNLFNDKI
     DTYANKSLRA ISLAYRDIDS NVDISDFDAL FKDFTLVSIL GIMDPLRPGV KRAVQDCQGA
     GVVVRMITGD NIHTAKAIAA ECGIYHPRQE GVALEGPEFR NMSSDEIYHV LPHLEVLARS
     SPDDKQKLVK YLKAAGETVA VTGDGTNDAP ALKLADVGFS MGIAGTEVAK EASAIILMDD
     NFASIVKAIV WGRTVNDAVR KFLQFQLTVN ITAVLLTFVS AVVNEDGESV LTAVQLLWVN
     LIMDTFAALA LATDPPHPDV LERSPDSKRT GLISITMWKM ILGQAIFQIV VTFSLVFLGP
     SWFNVKNDID REQHNAMVFN AFVWMQFFNM FVNRRLDNKF NMFDGVLKNF WFMSIMLIIA
     LVQVLIMFVG GTAFSIVKQT RAQWTIALTC GLMSLPAGIL IRCIPDSWVL KLYPRSLVSV
     TGRLFIRLKN ALPFTQKSKV CNDEETFFIN SPSQHELNRF QYDLSDNNSQ TNLLNSDPTR
     GEDHYSTSST EGDQRESNYH IDNDSVDSLV DDAVSVGDLS NQGGF
//
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