ID A0A178AHJ8_9PLEO Unreviewed; 1082 AA.
AC A0A178AHJ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cation-transporting ATPase pma1 {ECO:0000313|EMBL:OAK96963.1};
GN ORFNames=IQ06DRAFT_282540 {ECO:0000313|EMBL:OAK96963.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK96963.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK96963.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK96963.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441719; OAK96963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AHJ8; -.
DR STRING; 765868.A0A178AHJ8; -.
DR InParanoid; A0A178AHJ8; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000077206; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
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 141..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 837..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 971..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1031
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1037..1060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..165
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..605
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 119855 MW; 9033A4D36A59F9CB CRC64;
MNTNPPRIVW DDVERGARGR SDRRDTRQLS RSQSRNSISS VRSRTQSVSG IPIGFRTLSI
QVSESQAKAS EPPPKQSKNT DDENRDYFGQ LQYHTLSTKE VCDRFNVFQE QGLTTEAAAT
RLQRDGKNEI PSPKDHVWRK VFWYVFGGFC SILWVGVVIF FICWRPLGDP NPAAYNLGLA
ILVIIVILLQ ASFSAFQDWS TKRTMKSILD LLPSDAFVLR GGAFVKVPST DVVAGDIVRI
SIGNKVPADI RLLTSSGDIR FDRSMITGEA EEVDGAVDST DPNFLESRNI SFMGTMVVNG
SAVGVVVLTG KNSVMGRIAQ ATSGVKDEPT LIQREISRFV RIIVCLTAFL ALLLLFTWIG
WLRVDHKGFL SLIAMLNNVM GCVVAFIPEG MPVGVALTLM MIARRMKSAS VLPKGLSTVE
TLGCVNVICS DKTGTLTENK MTVTSVCFLD ELKPADELAQ KLATVSCPEP LQMLHRTALL
CNDAMFDPTT NHLPVAKREI QGNATDGAVL RFAEGAQRGK GIQDAFPRVF SIPFNSKNKW
MLSLHKEGAS SETAKGQQYL VLVKGAPDVL LSKCSSWLSF HSNKVEELDD EARRLLSAAQ
ETLSRNAERV IMLCQRRYKP IAPLQSNAFS EELAEHALRD LTIVGMLGIL DPPRPESAET
VATCRRAGIR FFMVTGDFGL TGAAIARRIG IFSGDRDPDT IANVLSQAMS DESMGKDTQP
DGERNRALLL EGSQLNDLGE SGWDVVCAYE EIVFGRTTPE QKLRIVNELK QRHNVVAVTG
DGVNDAPALR ASDVGIAIVS GSDVALEASD LVLLDKFSSI VDGIRLGRLV FQNLQKVIGY
LLPAGSWSEI WPVLLNVFFG VPLPLSSFLM IIICVFTDLF CALALVMERE EFDLLSLPPR
NTKRDHLINI KIYVQSYLFI GVMETVSAHA MFFLYMWRHA KIPASALFFA YEKYADGFYG
YTEDELTHFN TVGQCVYFVT LVMLQWGNIL SIRNKRLSIL QADPIRKARR NPWLALSILI
SFCIAVFVTE VKGIQNLFGT AAVPIEFWLI PLPLALGILM MDEIRKLVVR TWPKGPIARI
AW
//
