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Database: UniProt
Entry: A0A1Y2ESD4_9FUNG
LinkDB: A0A1Y2ESD4_9FUNG
Original site: A0A1Y2ESD4_9FUNG 
ID   A0A1Y2ESD4_9FUNG        Unreviewed;      1212 AA.
AC   A0A1Y2ESD4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Calcium-translocating P-type ATPase {ECO:0000313|EMBL:ORY74480.1};
GN   ORFNames=LY90DRAFT_451548 {ECO:0000313|EMBL:ORY74480.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY74480.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY74480.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY74480.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY74480.1}.
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DR   EMBL; MCOG01000029; ORY74480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2ESD4; -.
DR   STRING; 1754190.A0A1Y2ESD4; -.
DR   OrthoDB; 847at2759; -.
DR   Proteomes; UP000193920; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
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   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        133..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        866..886
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        935..961
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1049..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1080..1103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..144
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
FT   DOMAIN          893..1101
FT                   /note="Cation-transporting P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00689"
FT   REGION          656..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1212 AA;  135033 MW;  F91C80E9606F9DD3 CRC64;
     MVNKGSTEKI DKEELIDSPF AYTKDELYSL CDPKNIKLLE EYGGVNGLFI GLQSSPTFGL
     SSSETDNFEK HVTREDCKIK KTSSEISILA SNIDSVHDNQ FCVRKKVFGE NKVPPVKQTS
     LFELMIAALS DKTMIMLCIA ACVSLAIGIY QDTTSDDDEP KVHWVEGCAI LVAVVIVVLV
     GSINDYNKEK RFRKLNEKKE DRMVKAFRDG QNTLISVYDV QTGDILLLEP GDIICADGVL
     IENQNIRCDE SSSTGESDTI KKSLNEDPFI ISGSKVLEGM GKYIVTGVGI NSFHGRTMMG
     LRVEQEETPL QAKLNILAEQ IAKVGALAAV LMLIVLIVKY VIVIILTNYC DDDNCTFQKV
     FSQVTNIVIA AITIIVVAVP EGLPLAVTLT LAFAATRMIK DNCLVRLIAS CEIMGSATVI
     CSDKTGTLTE NKMTVVEAVY GRNVHVAGDN EIRNSPKILS GLYINNPVMQ HGVLTGTELL
     KILLENISIN STAFENVDEE THQIVFIGSK TETALLNFCQ KMGGDYMAYR ESKYIKQIQT
     YPFSSERKSM TTLIEINLNS EGIEDHEPIY RVHIKGASEI VLGYCSHAMI LPHPKDRQGE
     AINQELNEKL LIDFNENVIR RFAENSLRTI CLAYRDLTKS EYKEILERVK KEIEQEEKEK
     REAKGENNEE NRTEHQHEID EETILSHPNA LKYLLEKNLV CLAIVGIEDP VREGVPEAIK
     ICQRAGVSVK MVTGDNIDTA RSIAKKCGIY TKGGIVMEGC DFRKLSSDEM DNIVGKLQVL
     ARSSPMDKQL LVQHLKDIGE TVAVTGDGTN DGPALKRADV GFSMGISGTE VAKEASSIVL
     MDDNFASIVK AMLWGRSVND SVKKFIQFQL TVNVSAVLLA FISSVIDGNE SGALTAIQLL
     WVNLIMDTLA ALALATESPS IDLLDRPPTL KNAPLISIPM WKMIIGMAIL QVIVGNVLLF
     LGPKMFKLTE LSDVGGIIKT RNNIKDYYNR NRAKIGRSFA KFEDTVDDQK KTIKTMVFNT
     FVYMQVFNEI NCRVITNELN VFKGIHKNAY FYCIFLFVAI AQFFIVQYGG TIFQTIKLNW
     WQFLICIGIG VFSLPFAVFL RLIPDKWFYC FFKNQEKIAP KEIDDEEIEA SNTSLNSSLD
     KTTLRVFRTV RGGRLLSLSS ITSLNGSQKI SYSNGSLNKS RRESIRKSQS IAIDIPKNDN
     SRQANIDDEE KN
//
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