ID A0A0L0HSY3_SPIPD Unreviewed; 1081 AA.
AC A0A0L0HSY3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Na,H/K antiporter P-type ATPase, alpha subunit {ECO:0000313|EMBL:KND04182.1};
GN ORFNames=SPPG_01615 {ECO:0000313|EMBL:KND04182.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KND04182.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KND04182.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KND04182.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ257451; KND04182.1; -; Genomic_DNA.
DR RefSeq; XP_016612221.1; XM_016749934.1.
DR AlphaFoldDB; A0A0L0HSY3; -.
DR STRING; 645134.A0A0L0HSY3; -.
DR GeneID; 27685267; -.
DR VEuPathDB; FungiDB:SPPG_01615; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; A0A0L0HSY3; -.
DR OMA; EACASWY; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000053201; 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; 2.
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 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; 2.
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:UP000053201};
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 71..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1031..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..98
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1081 AA; 119519 MW; CD8F72F12F13061C CRC64;
MESTGATDKK TKKVDLNEHL LSFEEIQKLH KTSFDARKPV ASAGLTPTEV TQRQAEHGPN
ILTPPKQKSL LLLYLECLAN LFNLLLLIAG VFTYILYGID PVGNYLNLYV GAILLGVALL
NAFIEFYQLQ KSAAILRSFM NMVPMKGHAI RGSALVDLPA AELVVGDIVF VRQGDKIPAD
IYVFHSSELK VDNSSLTGES DPQERTAHNT HKNPLEATNL AFSGTLAISG ECYGVVIRIG
DKTVLGQIAG LTQNEKKRPS PLSREIDDFV SIIATIAFIS ALIFFIVIMI KDKKINTAFN
FAIGVLTAWV PQGLPATMTM LLTIAAKRMA ARNVLVKDLR GVETLGAITL LATDKTGTLT
KNRMTVASIW TSLRILSADP HATNLEAEEG AFDQSISGVN EMLHLSAMCT RARFDRADVP
VPERNINGDA TESGLLRWSA QQLSDIDQLS AKYPKVFEVP FNSDNKWALT IHRKQHANGV
FTLYLKGAPE RVLKMCSVIL VNGKDVPLTS EHEQAFLKTY QWMAGKGRRV LAFAQLQMPA
EKYPENIEFS KEKENYPTRD LCFMGLISLE DPPKHGVREA IGRCREAGIK VMMVTGDHPL
TAEAIGRKIN LMLGHTKETL AKKTGRPIET IQEHEYSSIV IHGETIDDLT DSDWDKILMK
EEIIFARTSP KHKLEIVSRA QNLGHIVGVT GDGVNDSPAL KKADLGIAMN ISGSDVSKEA
ASMILLDDNF ASIVGGIAEG RLIFANLKKS IQYTLTHIIP EVVPFLLYAV VPLPIMLATL
QILVVDLGFE LFAALCFAWE PPESKEGLMK LPPRQPVTEE SIVRRRQYQA EDLQHGGGSS
EDLSELGFFE KLSKFVRAPF TLYYWKRKTR PANGEVLVDA GVLSWAYIEA AILETGGCIL
AFFVVLYNAK SAATGEPFRL TPYDAYNLQN NGGFVTGASD YITQSGHVLN ADDQLDALAQ
GQSAFYFCLM INQMWNLFAC KFKYRMPFGI YVFKNRYTFL SVLSGSAFTA FIVYAPPLNT
GFGTSYHLSP IYWLIGMASG ALIVAYSAVR KLLLRHFFPV TWNPAIEGLN MHPTRWSMIQ
G
//
