ID A0A409VD51_9AGAR Unreviewed; 1094 AA.
AC A0A409VD51;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=CVT24_008441 {ECO:0000313|EMBL:PPQ64539.1};
OS Panaeolus cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ64539.1, ECO:0000313|Proteomes:UP000284842};
RN [1] {ECO:0000313|EMBL:PPQ64539.1, ECO:0000313|Proteomes:UP000284842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2629 {ECO:0000313|EMBL:PPQ64539.1,
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:PPQ64539.1}.
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DR EMBL; NHTK01006085; PPQ64539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409VD51; -.
DR STRING; 181874.A0A409VD51; -.
DR InParanoid; A0A409VD51; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000284842; 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 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 412..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 993..1010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1022..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1071
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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 117748 MW; E3861CCDCBED8E02 CRC64;
MSSQNIKGSS GMGYERKKRN MTAIPITSPM ATSSSSSYRF VSGQHSAGPY RQGARSPSPP
ASAYFPLLSA DGNARLRPTP DAESHFAYST TLRRHQSDGA AALSSPAEFA AAVNAEASSL
WTRALNVITG RNEVEYQAVD NGRASPPLTS RPESKDTASG KFAHYTVEAT INYFRTSGTN
GLHHSDITTL RETHGYNEFS VASPEPLWLK FAKTIYESPL ILLLCGSATV SAIMGNVDDA
VSITVAVLIV LTVGFVQERR SEKSLEALNK LVPHHCHVIR EGEAIHVLAN ELVPGDLVKF
GMGDRIPADI RLVETVDLEV DESSLTGETE ARKKDTDMCK FDNGALTGEP VALADRTCIT
YMGTLVRNGR GQGIVIATGA ETEFGVIFSM MQDVEEKRTP LQLNMDELAK KLSMLSFGII
GVICLIGVLQ KRSWLEMFTI GVSLAVAAIP EGLPIVTTVT LALGVLRMAK RKAIVKKLHS
VESLGSVSVI CSDKTGTLTK NEQTVTEAYA VDETINLDPS SSIPYTGNVS PAIMRALDIG
ALCNNASLIR NEDGVYVGQS TDVALLNVLQ LFNLPDRRDT FRRLSELAFN SERKFMAVSG
IHEELPGANT GKLQVNGSPR ETLYIKGSIE AILERCKFYF VNEGSTPALD ASMRNVITTR
ANAAAARGLR VIAMAYGYGS AGGPTTASAS PSPSRAPSPQ LSETPNNLVF VGFQAMLDPP
RKGVADSIGA LQAGGVQVVM ITGDAEPTAL SIAQKLGLQT GRPGRDGSGT TVSSHHCLTG
KAIDTMTKAQ LKERVGTVSV FARTTPKHKM AIIEAFQARG KVVAMTGDGV NDAPALKMAD
IGISMGKSGT DVAKEAADMI LVDDNFSTIL PAVEEGKSIF HNIQNFLAFQ LSTAAAALTL
ITLSTMLGLD NPLNPMQILF INILMDGPPS QSLGVDPVDP AIMRRPPRKK NASIITKQLL
LRVLFSASII VVGTLFVYMF ALYDQDMSRR EQTMTFTAFV FLDLVSAVQN RGLNCALTQN
RMLVLTVSIS FLTQLALVYV GFMQAIFHTD ALPIRDLGVI LGLAATSFML HEARRWFERR
RDDDGWGGFM EEVA
//
