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Database: UniProt
Entry: A0A409W3D0_9AGAR
LinkDB: A0A409W3D0_9AGAR
Original site: A0A409W3D0_9AGAR 
ID   A0A409W3D0_9AGAR        Unreviewed;      1063 AA.
AC   A0A409W3D0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=CVT24_000298 {ECO:0000313|EMBL:PPQ72985.1};
OS   Panaeolus cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX   NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ72985.1, ECO:0000313|Proteomes:UP000284842};
RN   [1] {ECO:0000313|EMBL:PPQ72985.1, ECO:0000313|Proteomes:UP000284842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2629 {ECO:0000313|EMBL:PPQ72985.1,
RC   ECO:0000313|Proteomes:UP000284842};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PPQ72985.1}.
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DR   EMBL; NHTK01005842; PPQ72985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409W3D0; -.
DR   FunCoup; A0A409W3D0; 60.
DR   STRING; 181874.A0A409W3D0; -.
DR   InParanoid; A0A409W3D0; -.
DR   OrthoDB; 3352408at2759; -.
DR   Proteomes; UP000284842; 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:0030001; P:metal ion transport; IEA:UniProtKB-ARBA.
DR   FunFam; 3.40.50.1000:FF:000193; Plasma membrane calcium-transporting ATPase 2; 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; IPR059000; ATPase_P-type_domA.
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; 3.
DR   PANTHER; PTHR42861; CALCIUM-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   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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:UP000284842};
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        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        838..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        876..905
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        925..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        973..991
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1003..1025
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..111
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1063 AA;  113983 MW;  B449EA5D7C558408 CRC64;
     MGFFSKSSGT RLDSRSNTTI SVTVPPKNPD FASVAPTAHI TSVQDLLEDL GTSATDGLSR
     NEAARRLETC GENLLQGKGG VSAWKVFIGQ LTNALTAVLL AALALSFGVQ DFIEGAVIAA
     VIVLNTTVGF FQEYRAEKTM DSLRQLSSPT ATVIRNGESI AIPAKNVVPG DIVLVKSGDV
     IPADLRLVSS SNLEISEQLL TGESIPVAKN IDTFTSDQLD VPIGDRLNLC YASTIVTKGR
     GTGIVIGRIA SVISGATQES TSSEVDQLPW YKRFVERVLI FVGLRTGTPL QQKLVKLAFL
     LLGSAIILAI IVFSVARWKV TNTVALYAIA TAIAIIPESL IAVLTLTMAV GTRRMATENV
     IVRKLDALEN LGAVTDICSD KTGTLTLGKM SVRKLWVAAN PNDAEEYTAE VTQNALEPVG
     AVTKHDNTVV EPSAIHAGLA EVVRIASLCN VATVQKNLKG EWKSTGDPTE VALQVFATKL
     GLGRNTLTAD GATPEGTSGR PALGRIISNE KEAVKFDDEK PKNNKRFALI QEFPFSSEIK
     KMTTIYHDNE NPEEAIVLTK GAVERILDSS SFYVPSPNAP SVVAPLTQEI RNTFMVKAEE
     LASQGLRVIG LGSRLVPRDQ AKALKRDETE CDLVFKGLAG IFDPPRPETL GAVRACKAAG
     IVVHMLTGDH ITTARAIAQD VEIISPDAPA SAVMTAMEFD KLTDAEIDAL PELPLVIARC
     APETKVRMIH AGKRRGKHLS MSGDGVNDSP ALKLAPVGIA MGMAGSDVAK DASDLVLTDD
     NFNSIVVAIS EGRRLFTNIQ RFLLHLLAVN VAEVLVLIVG LCFVDGEGTS VFPLSPIAVL
     WVNMVTSSPP AFGLGLEKAS AEMMKKPPHS LKEGVFSWPM IVDCFAAGIV MGALGLASFV
     IVIYGKNGGN LAHGCNHHAT DVCNAVFRAR STTFAALIFC INLYALELKS LDRSMFALTP
     GQFFMKDIWA NKILLFSVLA GMVTVVLPIY TPGFSTKVFY QSGISWEWGI VIAASVVFII
     WIEIWKMIRL PLYKRWFNYG ATVGPSHHAS APTTMLSEKS GEV
//
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