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
//