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Database: UniProt
Entry: K5X088_AGABU
LinkDB: K5X088_AGABU
Original site: K5X088_AGABU 
ID   K5X088_AGABU            Unreviewed;      1107 AA.
AC   K5X088;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=AGABI1DRAFT_72076 {ECO:0000313|EMBL:EKM81196.1};
OS   Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS   10392) (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM81196.1, ECO:0000313|Proteomes:UP000008493};
RN   [1] {ECO:0000313|Proteomes:UP000008493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC   {ECO:0000313|Proteomes:UP000008493};
RX   PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA   Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA   Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA   Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA   Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA   Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA   Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA   Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT   "Genome sequence of the button mushroom Agaricus bisporus reveals
RT   mechanisms governing adaptation to a humic-rich ecological niche.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; JH971388; EKM81196.1; -; Genomic_DNA.
DR   RefSeq; XP_007328195.1; XM_007328133.1.
DR   AlphaFoldDB; K5X088; -.
DR   STRING; 597362.K5X088; -.
DR   GeneID; 18831003; -.
DR   KEGG; abp:AGABI1DRAFT72076; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   HOGENOM; CLU_002360_3_1_1; -.
DR   InParanoid; K5X088; -.
DR   OMA; KMHACET; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000008493; 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   GO; GO:0030001; P:metal ion transport; IEA:UniProt.
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; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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; 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   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:UP000008493};
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        215..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        446..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        970..992
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1033..1053
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          161..236
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1107 AA;  119699 MW;  957D59A1BC7013C1 CRC64;
     MGFERKKRNL TTIPITSPVG SSSGYYRQQG PTPNPHAMTN VRNPNRTPSP PASAYFPLLS
     GDANAQLRPT PDADIHFAYS TTLRRHHSDG AALTSPGHFA AAVEAEATSL WKRALLTVTG
     QPLPETPGLE NGLPTTRPAD PRPPPSAGTL QEEKKDTISA KFAHYSVADT VAWYRTNATT
     GLLHSDIAHL QGQHGYNEFS VAAPEPLYLK FLKTIYESHL ILLLCGSATV SAIMGNVDDA
     ISITVAVLIV LTVGFVQERR SEKSLEALNK LVPHHCHVIR QGETLHVLAN EIVPGDLVRF
     STGDRIPADI RIVDAADLEI DESSFTGETT ARRKFSEPCA YIDGGSVDGI PGQSVALADR
     SCIAYMGTLV RNGHGSGIVI ATGEETEFGV IFSMMQEVEE RRTPLQLSMD ELAKRLSILS
     FGIIGIICLI GVLQQRSWLD MFTIGVSLAV AAIPEGLPIV TTVTLALGVL RMAKRKAIVK
     KLHSVEALGS VSVVCSDKTG TLTKNEQTVT EAYAVDETIY LDPSSATQYT GTISPAMRKT
     LEIGALCNNA LVERNEEGLF VGQSTDVALL NVLHLVGITD RRASFKRTSE KPFNSEQKYM
     AVSGIHMDST FSSSSEHLRP PPNGTINANS REMYYIKGSI EIILDRCKFY YVNEESTPGL
     DEETRKAIMT KAQSTASRGL RVIAMAYGYG NVDSFHNSSR SPSRASSPIH THGGEKDHLV
     FVGFAAMVDP PRKGVADSVG LLQAGGVHVV MITGDAEHTA LAIAKDIGFR VGRQLHPLEG
     AGQRYSGVLT GKAIDRLSKA QLKEIVGGIS VFARTTPKHK MRIVEAFQSR GAVVAMTGDG
     VNDAPALKMA DIGLSMGKSG TDVAKEAADA ILVDDNFSTI LPAIEEGKSI FHNIQNFLSF
     QLSTAAAALT LITLSTLLGL DNPLNAMQIL FVNILMDGPP SQSLGVDPVD PAVMRRPPRR
     KNAPIITKRL LYRVIFSASL IVMGTLFIYT FALEDSDVSR REQTMTFTCF VFLDLVSAVQ
     NRGLGCGLLQ NKMLVATVGI SALTQLALVY VPFLQAIFQT EALRGRDMGV IMGIAGSSFG
     LHEVRRRWER RQEDKGGYES VAMEELA
//
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