ID A0A0B2X183_METAS Unreviewed; 1531 AA.
AC A0A0B2X183;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=MAM_03287 {ECO:0000313|EMBL:KHN98825.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN98825.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHN98825.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN98825.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KHN98825.1}.
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DR EMBL; AZHE01000006; KHN98825.1; -; Genomic_DNA.
DR STRING; 1081103.A0A0B2X183; -.
DR HOGENOM; CLU_000846_0_0_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000030816; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000030816};
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 149..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 521..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 566..591
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1151..1167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1179..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1230..1251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1271..1289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1336..1356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 121..171
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1116..1365
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 884..915
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 172941 MW; 567413D9DF169ADB CRC64;
MSPPTSPDPG PDAMLSNAQT QRARWATRKM TVKSSRTKRL SLLNRVHRRM HSEKSVTGDD
GNGAPFEDRD PHHNGGGDEH HSDDPQDETD DESDDEDSTR TLYFNMPLPD DMIEDGRPIY
SFPRNKIRTA KYTPLSFIPK NLWFQFHNVA NIFFLFLVIL VIFPIFGGVN PGLNAVPLIV
IIVLTAAKDA IEDYRRTILD IELNNASVHK LHNWNNVNVQ EDNVSTWRKF KKANSRFFGS
IWHAVESLWS KKARTRRAER KERKRNPQME EEARPSIETV RTRRSIRESI ASPFGNREPF
VDAQEEIQMT PVPSPTPANG VPHVQFPDLE DARRAAAIQD MKSDLINYTK PSKGARFNKD
TWKGLKVGDF VRIYNDDELP ADVIILSTSD PDGACYVETK NLDGETNLKV RQALRCGRSI
RHARDAERAE FRIESEAPHP NLYKYNGAIH WQQAVPGYPD DDPEDMTEPI TIDNLLLRGC
NLRNTEWVLG VVVFTGHDTR IMMNAGITPS KRARIAREMN FNVICNFGIL LIMCLLAAIV
NGVAWAKTDA SLHFFEFESI GGSAPMSGFI TFWAAIILFQ NLVPISLYIT LEVVRTLQAI
FIFSDVEMYY EPIDQPCIPK SWNISDDVGQ IEYIFSDKTG TLTQNVMEFK KATVNGQPYG
EAYTEAQAGM QKRMGVDVEK EGARIQAEIA EAKVRALQGL RKINDNPYLH DDALTFIAPD
FVSDLAGENG QEQQSAIEEF MLALALCHTV IAEKTPGEPP KMTFKAQSPD EEALVATARD
MGFTVLGHSG DGINLNVMGE ERHYPILNTI EFNSSRKRMS SIVRMPDGRI VLICKGADSV
IYARLKRGEQ QQLRRETAEH LEMFAREGLR TLCIARKDLT EAEYRSWKKE HDEAASALEN
REEKLENVAD MIEQELYLLG GTAIEDRLQD GVPDTIALLA KAGIKLWVLT GDKVETAINI
GFSCNLLSND MELIHLRVEE DESGETSDDA FLENVEKQLD QYLQVFGITG SDQDLALARK
NHEPPGPTHG VVIDGFTLRW ALHDKLKQKF LLLCKQCRSV LCCRVSPAQK AAVVAMVKNG
LDVMTLSIGD GANDVAMIQE ADVGVGIAGL EGRQAAMSSD YAIAQFRFLQ RLVLVHGRWS
YRRLAESISN FFYKNMVWTF AIFWYEAFCD YDMTYLFDYT YILMFNLFFT SVPVAIMGVL
DQDVSDKVSL AVPELYRRGI ERLEWTQKKF WLYMVDGIYQ SVMVFFIPYL LFIPAKSVTL
DGLGLEDRLR FGAYVAHPAI LAINGYILIN TYRWDWLMLL IVVISDVFIF FWTGIYTSFT
SSGFFYNTAA QVYGEATFWA VFFLVPVICL FPRFAIKALQ KVYWPYDVDI IREQELMGRF
AHLDKGAAGE ADSAESSSGK SGSESPRKAK HMTYGSVDED LRPIYPPSTA TRATTHNRTQ
NGSDSTNYTA NRMSLDVPAQ GRHSTERARP SYDRMRMSMD RVRPSFEASN DFTSAARLSR
IESSQSHAQP PQGGRFKARL RGLSLTKSAN V
//
