ID F4RHY1_MELLP Unreviewed; 1377 AA.
AC F4RHY1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=MELLADRAFT_124106 {ECO:0000313|EMBL:EGG07902.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883102; EGG07902.1; -; Genomic_DNA.
DR RefSeq; XP_007408667.1; XM_007408605.1.
DR STRING; 747676.F4RHY1; -.
DR EnsemblFungi; EGG07902; EGG07902; MELLADRAFT_124106.
DR GeneID; 18926614; -.
DR KEGG; mlr:MELLADRAFT_124106; -.
DR VEuPathDB; FungiDB:MELLADRAFT_124106; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_0_1; -.
DR InParanoid; F4RHY1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000001072; 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; 2.
DR PANTHER; PTHR24092:SF214; 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 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.
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:UP000001072};
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 534..556
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 586..608
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1098..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1125..1151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1172..1194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1209..1230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1237..1260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1280..1299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 269..336
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1058..1310
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1377 AA; 154589 MW; 923D3347CBC14DDA CRC64;
MSNHILGDDE SDDDFGAFNS QHQQHQQYRP TIQINSNPSS RQVPQDPFSP LEYHQNPLES
HQPYYHSSSH HLQEGYHPHS PADEEDTVFQ SERKHQSTST GISGFEQDQN PASYSGGNPS
NPLGTMQDLS HSQQAPAYQP FFDESDSPQE HHRNMSSNSN GLYASLANRR RSTLPNSSSM
ESGLPLSYTG AMPAGIPPPS AQGSKWALED DYEDDLSGIR SIPLVDAPGG PSNTSSKWAQ
QKTKQPSMKQ RITDLFSRQP KELTGERLIY LNDVARNERE FKYMSNYVST TKYNVVTFLP
KFLLEQFSKY ANLFFLFTAC IQQIPNVSPT NQYTTIAPLS LVLLVAAFKE MTEDIKRRNS
DSELNARHAQ VLVGSSFVEK PWRDIKVGDV VRLESNQHFP ADIVLLASSE PDGLAYIETS
NLDGETNLKI KQAHPSTSNL TSPSMVASLS GHLRSEHPNN SLYTYEGTLT IQSHGNSEKD
IPLSPDQMLL RGAQLRNTAW MYGLVVFTGH ETKLMRNATA TPIKRTAVER MVNVQIVFLF
IILLVLSVGS SAGSFIRTYS NSGQMWYLLE PATAGGGKLT TFIEDILTFI ILYNNLIPIS
LIVTMEVVKF QQAVLINSDL DMYYSVSDTP ALCRTSSLVE ELGQIEYVFS DKTGTLTRNE
MEFRQCSVAG IAYADIVEEH KRGEVFSFDD LAKNLQKGDD RSKVLSEFLT LLATCHTVIP
EEKDGKVIYQ ASSPDEAALV AGAEVLKHRF TVRKPQSIMI EVNGRQQEFQ VLNILEFNST
RKRMSSIVRA PDGKIKLYCK GADTVILERC AAHQPYKDST LVHLEEYATE GLRTLCIAMR
DIPEEEYKPW SAIYDKAAGT VNGRTEALDK ASELIEKNLF LLGATAIEDK LQEGVPDTIY
TLQQAGIKVW VLTGDRQETA INIGLSCKLI SESMSLVIVN EETSDATNEF INKKLLAIKS
QKNVGDLEEL ALVIDGKSLG FALDRSMSKS FLELAILCKA VVCCRVSPLQ KALVVKLVKK
NVKGSITLAI GDGANDVSMI QAAHVGVGIS GVEGLQAARS ADVAISQFRF LKKLLLVHGT
WSYVRLSKLI LYSFYKNITL YLIGFYFSFV NGFSGQVLFE SWTLTFYNVI FTVMPPFVLG
VFDQFVSARM LDRYPELYTL GQRNVFFTRR IFWEWVATAV FHSIIIFFFT AVIFNQDLIL
NQGWISGQWV WGTTAYLVTL MTVLGKAALI SDLWTKWTLL AIPGSFALTM IILPLYATIA
PKIGVSKEYY NLMPRMLSSP VFYLALFLIP VTCLIRDLAW KGYKRLFRPE SYHVVQEIQK
FNLPDYRPRM EQFQKAIKKV RAVQRLRRNR GFAFSQTEEG QEQLIRSYDT TIQKAKG
//
