ID A0A0F9YR62_9MICR Unreviewed; 997 AA.
AC A0A0F9YR62;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cation-transporting atpase {ECO:0000313|EMBL:KKO75037.1};
GN ORFNames=AAJ76_3500034361 {ECO:0000313|EMBL:KKO75037.1};
OS Vairimorpha ceranae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=40302 {ECO:0000313|EMBL:KKO75037.1, ECO:0000313|Proteomes:UP000034350};
RN [1] {ECO:0000313|EMBL:KKO75037.1, ECO:0000313|Proteomes:UP000034350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA08 1199 {ECO:0000313|EMBL:KKO75037.1,
RC ECO:0000313|Proteomes:UP000034350};
RX PubMed=25914091;
RA Pelin A., Selman M., Aris-Brosou S., Farinelli L., Corradi N.;
RT "Genome analyses suggest the presence of polyploidy and recent human-driven
RT expansions in eight global populations of the honeybee pathogen Nosema
RT ceranae.";
RL Environ. Microbiol. 0:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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:KKO75037.1}.
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DR EMBL; JPQZ01000035; KKO75037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9YR62; -.
DR VEuPathDB; MicrosporidiaDB:AAJ76_3500034361; -.
DR VEuPathDB; MicrosporidiaDB:G9O61_00g018810; -.
DR VEuPathDB; MicrosporidiaDB:NCER_101005; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000034350; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000034350};
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 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 860..879
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 899..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 971..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 997 AA; 113711 MW; 751A1FD6B5A964F1 CRC64;
MKNCFYRVRP LWKRVYVYPI YVLPVLIRLT NSFHVVPLFT ILFAIFLSLL TCWSDKIKIL
FTADLSNKPT HILFNGKLCL ISKNTFIFNR SKYLIEQGNI IQLVPDTKKR FKFYKSEYKT
HSYVEDRFLQ HWPKNYFSIE SPTFVKMFSQ HATTPFFVFQ VFCGILWCLD EYVYQALFTL
IMLVAVEAGL VFQRIIIMKQ FKTMNHKTVK IDLSTEKGIK QIDSYDIIPG NIIRIKSCIK
VPCDLLLLRG ACAVNEAILT GESVPLTKED IVEVEDQRIF DFEKDKKHVL FAGTEIIKLD
NNVIECFVLN TGFDTVQGKL IKKMMCNEEI TVNDIEAFGF IGMLLVFALV AAIYTCKEGL
KMGKSGYKVF LECILIITNV VPTELPLELS MAVNSCVSAL KELGIFCLEP FRIPYAGKVN
VCCFDKTGTL TETALDVSQI KFTTPFTADV LRTCNTLINL DNKITGDPQE VAIYEYMNKI
VLKSNNITLS EDFAVLDKLF IDTTNKTFQY KYTIKKKFLF SSELKRMTVV YECNKETYVS
MKGAPEVIKN YLVTVPDCYD DYEDYAKNGY RVIALAHKPF KKRTPFNRAE VEENLHFAGF
ILFDCKIKEH AKETISDLQN SGHKVVMITG DNILTALAVA RKLGIINSDD DKVGVEGKDI
DKVLSLDIFE QYKVFARADP EHKEKILERY NKKGYFTLMC GDGTNDVGAL KSAHIGVALV
EAQISTKPKI VIKEHSTPKQ ALLQKIAGEM NDQTQIKMGD ASVAAPFTAK TKSLECILNV
IRQGRSALVT TIQMYKILAL NSLVNAFSLS VLDCMGIRYG EYQLVVSGLL VALAFTFLSK
NVPLKEISKK RPLTTIFSKY MMLSIFLQVI VHIFSYLIVL KRLKCVETIV YEEKFKPSVT
NTALFLLSTS QQISTFLVNY IGRPFRESLV ENRKLMGCLC LLYGIIFYIL FDVNEEFSSM
MEVISLDSLK SFLLFVIITD LGVCFFIEKI CFRLFMI
//
