ID A0A1Y2AY62_9FUNG Unreviewed; 1607 AA.
AC A0A1Y2AY62;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=LY90DRAFT_513636 {ECO:0000313|EMBL:ORY26825.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY26825.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY26825.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY26825.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORY26825.1}.
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DR EMBL; MCOG01000198; ORY26825.1; -; Genomic_DNA.
DR STRING; 1754190.A0A1Y2AY62; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000193920; 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 Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 2.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF150; 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:UP000193920};
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 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 398..419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1029..1048
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1060..1081
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1111..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1149..1168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1175..1195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1215..1233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 54..104
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 997..1244
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 204..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1607 AA; 183137 MW; 738385AC9630EBCF CRC64;
MGLLRRATTE FSIRSHTENS EFFSSKDGAE GKRRIFINIP MEIPWIKSNG LPRVQFPNNR
IFTSHYTWYN FIPKNLFEQF RSVANFYFLI LVILQLLPQF QYGSSPITTA APMLFIVGVT
ALRAGFEDYK RHETDHKRNW MKTIKLGGWK NQNYIIQSQS KLKLLYQKIV AKLSFRPYHE
DDNIEDNTAS EIPLMELNEE FSSSEHIKSR SSSFNKSTTS LNSMKSNRHS IKNEIPKWIG
TTWQDLHVGD FVLLRENDLI PADILVISTS EQDNLCYIET KNLDGETNLK VRQGIKEFGG
IKKTNDLASI KCYLDADAPN NNLYTFKGVL HMVDQDTGEE TQNLCTINSM LLRDCILKNT
EWVIGLVVYT GFHTKSILNT GDSPSKRSKI EKQLNPQVLL NFLILAIMCI VCAVTHYLYT
ASFKSENAQF WTGDDNSDGN ESPIIAAIKT FINSLILYQN IIPIALYVSV EISKTLHAFF
IYSDEEIYDE ELEKPTLARS WNLSDDLGQI EYIFSDKTGT LTRNVMNFRK CTINGVLYGD
AYVTEAQMGQ NKANNVAVNA DDSEKQFEDE MVEMHKLMKS VFNPIYVTDK PTFADANLYK
DIIEDGDQAS FIKEFFILLA TCNTVLTEVK KDEDEVNSKE EDEDPLHNID ESLMSEDSHD
AKLLSYRAQS PDEGALVEGA RNLGFTLIGR NQSKLMLDVL GEQQTYEALQ VIEFDSDRKR
MSVIFRTPDN QIIIFCKGAD SVIFERLAAG QDKIKEVTLD HLQRFASEGL RTLCLGYRVL
NEEEFMDWHK RYKEASLLDS EEAQQQIALL NDEVENNFIL IGASAIEDKL QDGVPECIET
LSKAGIKIWV LTGDKLETAI NIGFACNLLN HNMQIIVIRG DDEEDTYNQL VKALSSFWAE
DGTDISGNPY SLVIDGQSLK HALGRRSKAL LLELSCRCKA VICCRVSPLQ KAKVVSLVKK
GLGAMCLAVG DGANDISMIQ EADIGVGISG KEGAQAVMSA DYAIGQFRFL TRLLLVHGRW
AYMRTANLIL TYFYKNVVWL FVLFWFQFNC GFSAAVLFDY NYTLFFTTVF TLLLNMNMGI
FDQDINDRIA IAIPQLYSIG ISGSLYTMQK FWVHIAYGIY ESLIAFFFGY FIYREATTSP
DGYDSGQEVM GNCVAFLLII SINIVMAFNT YSWTIITFGS LILTLAVWIG FVFYYSSYSS
SLTYGIISRL FGEPAFYLIT PVYFVLALAP RYIKKYIQVT HFPTDVDIIH EVNKYRIRIP
DLPENYEFDD ETYREKKKKK EKKREERRRA RDLYWKKQKE NFQKMVNILT PQSKTGDVKA
TYTSTNGTNN GSKYQFSTTE GGENGSVPII KVNPSNLLNP NDDASSQHST ATRKTKLFPS
NVRTPTFSSI HSSNSNSNAG VDTGTDGAGN EDELENAIQT PQQKYIYNIL KNQAIMKVLN
SHFPKLKVKD YIHTANKRRP SNAGIVYMND EKIVSNTGFC YSQESGMKEI ITPSGNENIL
PSYETMRGGE RTEWDNSIPK YKNFRRTRSL NDSYSRSRPE KLETRRYRTY QNNIFSKSVD
NFEYHRRLQQ HNSLKSPSDT EGFFNGNSNN NNNKNSIRKS KGKSSEY
//
