ID A0A0D0DZM1_9AGAM Unreviewed; 1061 AA.
AC A0A0D0DZM1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Unplaced genomic scaffold scaffold_438, whole genome shotgun sequence {ECO:0000313|EMBL:KIK92629.1};
GN ORFNames=PAXRUDRAFT_829771 {ECO:0000313|EMBL:KIK92629.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK92629.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK92629.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK92629.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN825260; KIK92629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0DZM1; -.
DR STRING; 930991.A0A0D0DZM1; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; A0A0D0DZM1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000054538; 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 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; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000054538};
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 105..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..915
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1022..1040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..129
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1061 AA; 116622 MW; AE8CC6D982561309 CRC64;
MEKAPGSSSV SRKSTERIPG YGIQIGYRTL SIRVDEKDLP GKSKKSADPA DAIAAIDVHL
ITTDEVYTRY SCSPNVGLEP AAVQRRAKDG KNIISPPPTQ YWMKALNYVF GGFNFLMWIA
FIVTLLSYKP LGQPPAVFNL GVAVLLMLVI IVSTTFYALV DWNASRIMKS IRSLIAQDAA
VIREGKQQII LANDIVVGDI VVLASGDRVP ADLRIIQMSS DLRFDRSLLT GESDMIPGSL
DATADNALET RNLALTSTFV TQGNCLGVVF ATGDRTVMGR LVKMSGETKF KLTTIQKEIW
FFTKVISSVA LSLFCLSLLL FGVWLRTSYP GYENVSMAII NSIGCLTAFV PQGLPVCVAL
SLTVIARRMA KRQVLVKNLA TIETLGCMSV LCSDKTGTLT AGKMAVESVA FFDAQIQAKG
INEKVSELPE PRLFAGLDAL HKIARLCNGA KFDSATASRP IEDRVVKGDP TDTALLRFSE
VLSVPALGID TPSMLSGFRR LFEIPFNSRN KWMLTVVQDN EALKNEISDK NAGIWMFVKG
APDMLFDSCS SVMKANGTVV PLDDFAKQHI SALQSKWSSE GQRVLALCRK PLDVFKSELP
PNDLEEIMYN EMRNLTLIGL VGIRDPPRSD VPTAIDVIRK AGVRVFMVTG DFKLTAVAIA
RQVGIITQHH FDTIDDVRAA ASHKYAEDIH LSAVKPSDDD PIRALVLTGD DVASLSPADW
NVIVGSYTEI AFARTTPDQK MKIVENIKAR GDNTVAVTGD GVNDAPALKA ADIGVAMGSG
SDVAKEAAAL VLLNNDFASI PVAIEMGRLV FDNLKKVTLY LMPVGSYTEF MAVLSNVLLG
MQIPLSSYLQ VCFSITNDVV MSTSLMYEKP EADLMLRKPR NARTDRLTDW RLFFQIYLFI
GLMTWPCAMG MFFLFMEQNG LTFYDVILVY NKWGEGWQGY TLEQLTQLVN TGQCIYYVTM
VFMQYGVLLS IRNRRVSILQ SNPLWGPRKN LIVPLGMIGT MLIAVTNLYG PGLQGVFSTT
PIPAMFWGPP FGFALGILMV DEVRKLIVRT YPKSIIAKMA W
//
