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
//