ID A0A1Y1WIC4_9FUNG Unreviewed; 1423 AA.
AC A0A1Y1WIC4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=DL89DRAFT_255255 {ECO:0000313|EMBL:ORX73115.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX73115.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX73115.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX73115.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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:ORX73115.1}.
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DR EMBL; MCFD01000002; ORX73115.1; -; Genomic_DNA.
DR STRING; 61395.A0A1Y1WIC4; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000193922; 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; 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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
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; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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:UP000193922};
KW Translocase {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 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 373..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1016..1035
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1047..1068
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1139..1161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1181..1201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 52..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 984..1211
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1423 AA; 159503 MW; 7ABF277198630F98 CRC64;
MAKTRGGQKP SILSRILGRK RKAGEPDSEP GAERTVYVNT PMPGSAYDEH GRPTHYPLNQ
IRTAKYTVVS FVPKNLFEQF RRVANMYFLF LLILQFIPAV TTGSPGLSAF ALFVIVALTM
AKDGYEDSKR SQSDKEANQA PAFVLGNAWV NTNKPPAGFF RPRGIMRLLW SDSGADGSVG
GAVGPSNTLP VGPGASGFAS TSYRPGSHGE RSDEDVGIGS SSWLQTEWRH LHVGDIVLLR
EGDAVPVDLV ILSTSEDDGT CFIETKNLDG ETNLKSKQST GNTAHLVMPQ QFADFQAPCK
SSLTVGTIFQ SPKPAAGSRD PLNVDNLLLR GSVLRNTRWA VGVAIFTGDD TKIMMNAGET
PSKRSRIERM MNYQVLSQFC LLFVLCLVSA IVGGIYYGKS QSFQQAFIVR YQTSTNQSAP
YFGFLDFWTM LILYQTVVPI SLYVTIEVVK SFQAYFINQD IDMYYARTDR RCIPKSWNLS
DDLGQVEYIF SDKTGTLTQN VMEFRQCTIR GRIYGEIVGD DEAERAAELR RSMQAKMATF
FDNPYRHSDT TTFLDTGIYD DLRADNIQAR AVIEFFTVLS LCHTVISDTP DPANKDYIEY
KAQSPDEAAL VSTARDVGFT FLRREKDRLF CNFLGHQQTY TLLATLEFTS ARKRMSVVVK
REDGRLMLLS KGADSVIMER LRSNQDRLVQ ATLDDLELFA NHGLRTLCLA YRLLDVQEFE
EWKSEYDQAM SSLGDRDQEV EEVCEKLERD LQLIGGTAIE DKLQDGVPET ISQLALAGIK
LPRTRSQRET SWSGRCASLA IRTLDLSFRG GGGGDVMAGA QPKESTSSWR ALLRPVTDHR
KHKKKHGKQP SAFQHARDVA QNKNHRKGIK GIWDDVRTRN IPEERKQGLT VKHDAPLGLV
IDGHSLKYAL EPDISPLLLE LAVRCQSVVC CRVSPLQKAL VVRLVKEGLG TLCLSIGDGA
NDVSMIQEAD VGIGISGEEG LQAVMASDYA IAQFRFLQKL LLVHGRWSYL RITSMILNFF
YKNVVFTIAS FWYQIYCQFS GQNFFDYTLI TLYNMFFTSL PPGVLGVFDQ DLPAAIGMVV
PQLYKRGIYK LEYSMARFWM YVRSAMAWTH RNKDDVGTVG AFCVVFTTNM YMLMNNRTFT
WVMPLAQLIG VGLLFAVFFL YGVMYDTSFS AGAATRVFAQ ANMWLLLVLT VTACVLPHYI
AKFVRSAWYP TDTDIIREIV HAFHKRTASL VGGESTLPSP THHKEMPFGT LPTRSGSTQH
RHSLRRPSSP DSPGMAGAIP LDDFPVHSPP RRTARQTEEA DYDFSKIVSY PETDTAMINR
LHRLSHVEAS GFEGSNILKR MSVHQKSRHH GARAMAEDIS EENDDVYQMS PLQRAASRAS
MRSSIYYLDD GTLEPYTGYA FAQEEENVRE RKQKGKKQRR PGF
//
