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Database: UniProt
Entry: A0A421D0N3_9EURO
LinkDB: A0A421D0N3_9EURO
Original site: A0A421D0N3_9EURO 
ID   A0A421D0N3_9EURO        Unreviewed;      1118 AA.
AC   A0A421D0N3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=CFD26_101975 {ECO:0000313|EMBL:RLL95676.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL95676.1, ECO:0000313|Proteomes:UP000215289};
RN   [1] {ECO:0000313|EMBL:RLL95676.1, ECO:0000313|Proteomes:UP000215289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL95676.1};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequences of two Aspergillus turcosus clinical strains
RT   isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT   other azole-resistant.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RLL95676.1}.
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DR   EMBL; NIDN02000142; RLL95676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421D0N3; -.
DR   STRING; 1245748.A0A421D0N3; -.
DR   Proteomes; UP000215289; 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; 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:UP000215289};
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        146..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        877..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        904..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        947..975
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1010..1027
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1048..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1079..1097
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..174
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  123438 MW;  A4C43E6F93245795 CRC64;
     MDATEQKSAV EEVARLRWQS EDEESGNQAR SSRPELIRSA SAASSSHVSD HSRKRTTVDP
     SVSLPIHYRT VSFDIEEAKE REEREKAIAQ SGVAADLSNL DWHTISVEEL QKRWQVDISQ
     GLSPNQVQER IRQYGKNAMS PLPHQWFWQI FGYFFKGFGA VLLIACILVF ISWKPLGEPP
     AVSNLALAIV LLAVFFIQAA FNAWQDWSSS QVMASITAML PESCLVMRDG SLAVVSALDI
     VPGDVVHLKA GNKLPADIRF VEVSNDACFD RSILTGESLP INGTVDSTDE NYLETHSIGL
     QGTHCVSGSV TGVVVSTGDA TVFGQIAKLS SQPKTGLTTL EKEVLRFVAL IVSIMLLMIV
     IFIIVWASWL RKDHPDWINV PTLIVDCVSV AVAFIPEGLP IALTASLTIT ANTMRKHKIL
     CKSLKTVETL GAVSVICSDK TGTLTKVITH FLSPSNDFHP ILRSPLTILQ NRMFVTDCAV
     SIATFTSDGA RDEMVLKGKS SAIHQLRAVA GLCNAAEFDA TTMNLPIHER KVIGDATDQA
     ILRFSEALGP VSELRGMWKK TYDLAFNSKN KFMVRTFSPV GGDLGHAMSP AESTEFRRDD
     TLLTIKGAPD ILIDRCTHVV SVDGSVQAMD RSTLNQLKQI KDQWSSEGKR VILLARKIFG
     AGHIQGSPFS HLFEAEVMNQ VKSGLVLVGL VGMVDPPRDE IPDVIRTLRN AGIRIFMVTG
     DFGLTALEIA RQCGIVTAGV LVDDAKALRR FPSVNDDFNE KPRSPAISLS GSELMALNEH
     QWEQLCQYKE IVFWRTTPEQ KLRIVREFQA RDEIVGMTGD GVNDAPSLKA ADIGIAMGSG
     SDIAIEASDM VLLESFSAIV EAVQYGRVVF DNLKKTIIYL LPAGSWSEFW PVFANIYFGL
     PQVLSSFLMI IICCFTDCAA ATVLAYETPE ADVLLRPPRR PKKDRLVNWK LMLQAYGIIG
     MIETVCSFAM AFWYLQRNGI PFSALWFGFG AVPANVNPDY FTARLNEASS VYFINLVVMQ
     WFNLMAIRTR RLSIFSHPPA FNKKTQNLLL FPAILFALGI AVFWLYIPAF QNALATTSVP
     AENYFLPAAF GLGILILDEL RKAAVRRWPD GILAKMAW
//
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