ID A0A197JLG0_9FUNG Unreviewed; 1099 AA.
AC A0A197JLG0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cation-transporting ATPase pma1 {ECO:0000313|EMBL:OAQ25985.1};
GN ORFNames=K457DRAFT_149972 {ECO:0000313|EMBL:OAQ25985.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ25985.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ25985.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ25985.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV442072; OAQ25985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JLG0; -.
DR STRING; 1314771.A0A197JLG0; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000078512; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000078512};
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 108..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1029..1050
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1078
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..131
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 16..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 122007 MW; A10F553E01A27144 CRC64;
MERAKGHAVP IEFRTLSLQV TETQRSNKTG DFKTSKGKNK NKDDDVAEPE TDFFSTIDFH
KLTIPEVSLR FNTNETLGLS QAEAQRRLAT NGHNTLDTRK PNYIKKGLGY VFGGFCSVLW
VGVITFFVCW APILQPDPIP TNLALAILVI FVIFLQASFS AFQDYSTAKV MSSIMDMIPA
DCMVIRDGQL VKVPASTLVV GDRVSLSLGN KVPADLRLVQ ASNDTRFDRA VLTGESEAIE
GAIHYTDENF LESKNIAFMG THVVQGSCVG VVVLKGNDTL MGRINRLTTG RKEKVTIIQQ
EISRFVRIIV CLTIFLATFI LSYWAGFLNV KYHEFMPVNV LLVTLMGCVV AFIPEGMPVC
VSLTLMMIAR RMRSNNILPK ALTTVETLGC VNVICSDKTG TLTENKMFVT NIAFLDNEST
PDEARAKIEK QSNSKTLPLS EEAPSVIALR QLQLATLLCN NAKFDPETLN LPVPERTVHG
DATDSALLRF SAQVADSSDL APCFERTQEI PFNSRNKWMM SVYQGSAQNP QPIKVLFGSE
MMNAGMVANE KDSQLVFVKG APDVLLPHCT SFVSGLSNIG QPLTSEWSAE LSRIQMEWSR
QGKRVLMLCK GGFSPYLAAA RNNAGSSHNT AQQEELARQG LHELCIIGLI GIMDPPRPEI
RDTIVSCRRA GARFFMVTGD FGITAAAIAK QIGLFSSHRE PDTYEDVVDP SRKGAKNGLD
ASYDDLGVFE PGRPRFREGT SLLLTGTDLA RISPGEWDLV CAYEEIVFAR TSPEQKLKIV
TEFQHRDGVV AVTGDGVNDA PALKAADVGV AVVSGSDVAI EAADLILLGG FDSIPVAMRL
GRIVFQNLQK VIGYLLPAGS WSEIFPVLIN SFLGTPLSLS SFLMIIICCF TDGFPCTALV
MEQEEFDLLA LPPRNSKKEH LITAKIYLQS YVFIGSVMTF FSNMLFYMYI KEYTGVPFKD
LVFTYGNPNF QSRYPHIDDD MFNNYYVNTG QCVTFVSLVI MQWGNVLSIR NRRMSILQAD
PIRPKRRNLW LFAGMFMSLL MAIFVTEVPW INQIMLTNPV PIKYWFLPFP CALAVLLLDE
MRKLMLRTFP NSIFGKLAW
//
