ID A0A1R0GWR2_9FUNG Unreviewed; 1666 AA.
AC A0A1R0GWR2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-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=AYI68_g4561 {ECO:0000313|EMBL:OLY81337.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY81337.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY81337.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY81337.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
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:OLY81337.1}.
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DR EMBL; LSSL01002561; OLY81337.1; -; Genomic_DNA.
DR STRING; 133383.A0A1R0GWR2; -.
DR Proteomes; UP000187455; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 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 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:UP000187455};
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 234..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 638..660
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 680..701
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1392..1413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1425..1445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1476..1498
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1510..1531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1543..1562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1586..1607
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 204..259
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1361..1608
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 188072 MW; C8DDEC73128A90F9 CRC64;
MSPKNNLKDH DRKSFEHDNN SSESDYDDDP ETSNYENRIN KLKRYGVLRT KVTKLARNFN
PSAKSDLKPD GISFPLEIDL RRKSSENKRV ERKPTEILIR AENIKNRPSA EDSRESLSRP
SFVKPSRQSN ALVPDYALDG TPGISTHLDS GSSMSRAIPL PGYFLTEESD YWTGGYVFRL
RGKRPKEPIL VPGSITKRVH FEISYDYPKN SISTARYNIF TFLPAQLSSQ FSRIANLYFL
FIAILQQIPG WSTTGRFSTF LPLSIFVFFG IAHEGYDDYR RHKMDRAENT QKSRVLKVKI
NKSGPKTLQT RELHARSFRS SYSNRSSTIA TITRPLYFIW EWQRQMRERL VEKKRKKREQ
EDSDEEEEFD YDEVDRKYSS DLQAPSHPPP GILKEPTQKP PTGKLSMIFQ SLSHQTSSVS
HSPKNSVTEV DLDMSLDVEY PPIDTLPKLK KNKELAVMFS DEVQEHPAPD VVYSLPNNMS
CRWKSKKWQD LQVGDIILIG KDEWIPADCV VLATSNRDGN CFVETSSLDG ETTLKQKSAP
LVTSKAIKTS ENLSAFSGIT YTEAPSPDLY SFEGYLEVDG EKHALTPNNL LLRGSKLRNT
KFAVAQIVFS GEETRLRLNA TRNIRTKSPQ IQKTTNKIVI VVFSLLLCLC VVLSICAIVW
QHYVLPKHWY LIGADVPIAA IIFGNIVMLN ALIPISLYVT LEGVKIFQVY MMQKDIDMYY
EKTDTPMSAH TTAINEDLGM VKYVLSDKTG TLTENIMRFK AVMVGGLAFY HSNGADYEFE
NSSQNGSFSN STDSNTTSQG QFLSTPIPAQ GSFLDEYIFS DPVPHSPITV PNSDSSLSNS
TFYSNIDMDT NLCQLPPTSI LRKASAIDSS QSQRLSSSGI PFMSGNVGKM AEIFLKSMAL
CHSVQPDIDP STKILSGYQS TSPDEKSLVV AAAQLGYIVT ERNGPSLQIR IVESSRIINW
NNNLRKKGIQ DDDDTPSQLK LCPAQESDIV ETYQVLAVIE FSSARKRMSV VYRCPDGKIR
IFCKGADSVI LPRLAKAKPG DDETKWLHRC ADNSLRAFAC DGLRTLVYAH SEISEHEYSK
WAERFIAAST SLINRQERIE QVADELERNM LLTGVTAVED RLQEGVPETI EALRKAGIHV
WMLTGDKIET AINIAKSCRL IDGDEKTCHT MVLEGIKDVS ILAIELKRAN SILSTLSSYE
TRSMAPTKKR IRWPKVFRIS NKFFKVFKSL KISKGSKASG EPDVSEVALL DDSGTDDFDY
SNEKIERFAL VVDGDTISTL EDNPELMDKF IDVGILSDTI VCSRVSPSQK ALIAKHMRIR
CDSSNSYAVT VAIGDGGNDI AMIQEAHVGI GIAGVEGLQA ARSSDFSIAR FRFLRKLLFV
HGLWSYSRIS RFTLATFYKC FVFYTCQFVF QFFTGFSGTS VYESTALSMY NTLFTLLTVL
VLGTLDQDLC AKRLSGSPSY YSMIGPKNHL LNKKLFFTNV FMLGLCHIAI LSLGVFFIPI
RLSALFTSDL FSLSTFLFTV VIVTVNAKIS FIDTYTWSKF SHLAFWLSMA MWIIWNFMYN
VFTKDSVKSP YFSLNAWKYM LRSSQFWLII IIICFTALVV VLFWISISKS NDLTEIFRRR
MFNIDCSGRK REVIPSNKET DESIAETIQM DCMRSEISPI TARTKL
//
