ID A0A0D2AJ71_9PEZI Unreviewed; 1289 AA.
AC A0A0D2AJ71;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PV09_09295 {ECO:0000313|EMBL:KIV98963.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV98963.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV98963.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV98963.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847589; KIV98963.1; -; Genomic_DNA.
DR EMBL; KN847589; KIV98964.1; -; Genomic_DNA.
DR EMBL; KN847589; KIV98965.1; -; Genomic_DNA.
DR RefSeq; XP_016208833.1; XM_016363331.1.
DR RefSeq; XP_016208834.1; XM_016363332.1.
DR RefSeq; XP_016208835.1; XM_016363333.1.
DR STRING; 253628.A0A0D2AJ71; -.
DR GeneID; 27317268; -.
DR VEuPathDB; FungiDB:PV09_09295; -.
DR HOGENOM; CLU_000846_6_0_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000053259; 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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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:UP000053259};
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 209..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1099..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1148..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1190..1212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1219..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1252..1275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 180..232
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1036..1281
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1289 AA; 143285 MW; D75446C8ADF4B286 CRC64;
MSASHQYDQV NAPDFPDSDS ESDLNINLHE LDPQADWHLA GPSSNEHSRS RSYNMSDFGK
RIPLRNLRPG RQQHRIRVHD DNEVGEPPED GSEHHKHNRD SAASDDSAFD SAPLLLDAHT
SRRQRKPSGS TLARICSTWR ALSFNSPSGL PLGEALTDDE PEDEHDPSSN RIVLVGQRQP
TRYPLNAVSN AKYTPWSFVP RTLYNEFKFF LNLYFLLVAL SQVIPALRIG YLSTYIAPLV
FVLIVTLGKE AIDDIARRKR DAEANAEPYT VVQFQSRQSL DKSKRKSKTT ANGLEARNEQ
VDLQYSIKAS KDLKVGDVLK LSKNQRVPAD VVILQGISTD QSGSIDAQEL AGASEQQEQL
IHMEGQRVAA MSPLGDEERT RKDYAGETFI RTDQLDGETD WKLRLPSPLS QHLQLSKLIN
LKVTAAKPDK KVNEFVGMLE LDDEDVGFEP SEGQRMPQRA ALSLDNTAWA NTVLASSSTI
YAVVVYTGSQ TRQALSTSAS RSKTGLLDLE LNTLTKILCA LTLTLSGVLV LIGRIEGQEE
RKWYISVMRF LILFSTVVPI SLRVNLDMGK TVYAWFIEHD KGIPGTIVRT STIPEDLGRI
EYLLSDKTGT LTQNEMELKK VHVGTVSYAN DAMDEITSYV SQAFAPAEEG VLVTPSTPFN
VPATSTTRTR REIGSRVRDL VMALALCHNV TPTKEEVGGQ VRTSYQASSP DEIAIVRWTE
NVGLRLVHRD RNGMVLESHK SAKAVVRVRI LNTFPFTSES KRMGIIVQFL SSAASAVPET
CMDSEIWFYQ KGADTVMTSI VSANDWLDEE TVNMAREGLR TLVVGRKKLS ASQYQDFSLQ
FSQAAMALQG RDSAMSDVIR NHLERNLELL GVTGVEDKLQ QDVKPSLERL RNAGIKIWML
TGDKVETARC VAISSKLVAR GQYIHTITKL NRKDLAYDEL TALRSKPDAC LLIDGESLNI
MLTYLRNDFV SIAVQLPAVV ACRCSPTQKA DIAKLIRAHT KKRVACIGDG GNDVSMIQAA
DVGVGIVGKE GRQASLAADF SIHQFHYLTK LLVWHGRNSY KRSAKLAQFV IHRGLIISVC
QTVFSIASQF EPNALYRDWL LVGYATIYTL FPVFSLVLDR DVSESLAALY PELYKELKTG
RSLSYKTFFA WVAISIYQGC VIQGLSQLLV GVGRSATTTE SPVDEEDDKI FKRMVTVSYT
VLVINELCMV AVEITTWHPV MIVSIVGTAL TFFGSIPFLG DYIDLSFVVS GGFMWRLALT
LAIALVPVYA GKFIGRRWKP SSYRKVRGT
//
