ID A0A4P9YA18_9FUNG Unreviewed; 1145 AA.
AC A0A4P9YA18;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BJ684DRAFT_7889 {ECO:0000313|EMBL:RKP14890.1};
OS Piptocephalis cylindrospora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Zoopagomycotina;
OC Zoopagomycetes; Zoopagales; Piptocephalidaceae; Piptocephalis.
OX NCBI_TaxID=1907219 {ECO:0000313|EMBL:RKP14890.1, ECO:0000313|Proteomes:UP000267251};
RN [1] {ECO:0000313|Proteomes:UP000267251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; KZ987779; RKP14890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P9YA18; -.
DR Proteomes; UP000267251; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000267251};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 291..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 856..877
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 889..909
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 939..962
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 974..997
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1049..1068
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 27..93
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 825..1077
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 129699 MW; B406310BC28491D3 CRC64;
MKEFFGRFTQ GHGKSEKAGG PVESRRVAIN DQTTNLPRKF LHNRVSTAKY TIVSFFPKFL
YEQFSKYANI FFLFTSIIQQ LKGISPTNPY TTILPLCVVL IATAVKEVLE DWKHHQSDKS
ANACYTKVLL GDVFVDTRWR DVKVGDIVRI DGSEPFPADL VLLSSSEPEG LCYIETCNLD
GETNLKIKQS RPETAEMTSP SDISRLEGEL QCEQPNNSLY TFEGTLRRLQ PDGGIEELPL
DPQQILLRGA VLRNTTWVYG LVIYTGHETK LMRNAAATPI KRTSVERMTN VQILFLFALL
IILSVSCAAG AYYLQVHKAS ELRYTLLGSN FLDFLGNILT FIILFNNLIP ISLIVTMEVV
KFQQSALINS DLDMYYEPTD TPALARTSSL VEELGQIEYI FTDKTGTLTR NIMEFRECSI
AGLPYAETVD SSRKAREVDG EVVGVYDFLK LRDHLGGAHA SHRVIDEFLI LLAVCHTVIP
ERKGDNSEIT YQASSPDEAA LVAGAAGLGY RFITRKPRTV SLEVTKPDGR VEEETYEILQ
ICEFNSTRKR MSAVVRCPDG KVRVYCKGAD TVILERLAQN NPFVDATLRH LEEYATEGLR
TLCLAVREIP EPEYEQWSAL HHKASISMND RADELDRVAE LIEKDLFLLG ATAVEDKLQE
GVPETIHTLA QASIKMWVLT GDRQETAINI GYSCKLLQED MSLMICNEDS HWETKDFLEK
KLSLLRPSRS GLSATEPLAL IIDGHTLKFA LEKDIELLFL ELACMCKAVV CCRVSPLQKA
LVVKLVKKHK KAILLAIGDG ANDVSMIQAA HVGVGIAGME GMQAARAADF AIGQFRFLRK
LLLVHGAWSY HRLSKLILYS FYKNICLYMT QFWFSFYNGF SGQVIYESWT ISAYNVLLTV
LPPLVIGIFD QYLSARMLDR YPELYVLGQK SEFFNVRTFW AWAINGFAHS LILFFAAVAL
FGDGDFILTS GRTAGHWFFG TTLYTAVVLT VLLKAALVTD HWTKPSWMAI PGSFLFWMVF
FVIFGILAPM GGVATEYDGL VPVLYGSRIF WLFIIVTPIF CLLRDYAWKF AKRMYLPRAY
HYIQEIQKYN IPDYRPRMER FRNAVHKVRM IQRMKRNRGY AFSQNDEGEE KLIRAYDTTL
EKPRG
//
