ID B2W854_PYRTR Unreviewed; 1435 AA.
AC B2W854;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PTRG_05992 {ECO:0000313|EMBL:EDU48912.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU48912.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231619; EDU48912.1; -; Genomic_DNA.
DR RefSeq; XP_001936325.1; XM_001936290.1.
DR STRING; 426418.B2W854; -.
DR EnsemblFungi; EDU48912; EDU48912; PTRG_05992.
DR GeneID; 6344247; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_0_1; -.
DR InParanoid; B2W854; -.
DR OMA; GWFLWNI; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000001471; 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; 3.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 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 NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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; PF00702; Hydrolase; 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:UP000001471};
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 340..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 382..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1194..1215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1227..1248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1260..1281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1301..1322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 70..128
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1080..1329
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 48..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 160672 MW; B6063EE23E02A8A7 CRC64;
MGSGPVALPY YSSALKKKGP GRRSQMVRQA KDFAEQARKF IFRIKDVPPS KDGRHIQLDP
TRKEPPIDER TNQPYTSNWI RSTRYSAWNF VPRQLVAQFS KLANFYFLVI SILQMIPGLS
TTGQFTTIVP LMFFVTLSIA KEGYDDLRRY RLDKAENNRE THVLRVSQSD VRHSADNASV
PSSSSALQWE TIKWQDINVG DIIRLDRNEA APADLALLHT NGENNVAFVE TMALDGETNL
KSKQTTAAIS TTIIEQEDIL RTEAEFVVED PNRDLYSFEG RVTIHEKQAP LTLNEIIFRG
SILRNTPDAI GMVIYSGEEC RIRMNANKNP RIKAPALQGL VNRIVIVIVF FVLALSIFNA
VAYKIWQSHE DSMWYLAGTS VAFFPSFTSF IIMFNTMIPL SLYVSLEIVK LAQMFFLHTD
IDMYDPVSDT PCEPRTSTIN EELGQISYIF SDKTGTLTDN SMKFRKLSVA GVSWLHDADL
QSDEQKKKLI HKTRKKGKQP AKARKSFRST KDVSPGESAV PAFEATEQVE SPAEGGPSNW
RSNAKPGKAS RELRTQDMLR YIQRKPHTPF SKKARMFLLS LALCHTCLPE VQEDGKIDFM
ASSPDELALV QAAQDMGFLL INRDVHTITL KMPSGSDGES TQEVYEILDV IEFSSKRKRM
SILLRFPDGR ICIICKGADS IVLERLKLAT LANKKMVEIE RRANARKSME AQHAIARRSE
QADRRSSVAG RLSSVGGRRS MSFAQAARTS ANFGRPSFAA SVGARVSMSA RDEVDQWLRE
RENDRLGRPS VNEAIESTPI QTPRQSGLDR FSMAISEARS SIQLEEMEAM VDENIAGDDT
AVIERCLQHI NEFATEGLRT LLYGYRFMTE EEYQSWKRLY LDATTSLVDR TRLIEEAGDK
IEQGLDLCAA TAIEDKLQQG VPEAIDKLRR AKIKMWMLTG DKRETAINIG YSCRLIKEYS
TVTILDHEAS DLIQPITSAI HAITSNAAAH TVVVVDGQTL SKITASETLD PFFHELAILA
DSVICCRASP SQKAQLVKSI RKRVNKSITL AIGDGANDIA MIQEAHVGIG ITGKEGLQAA
RTSDYSIAQF RFLTKLLLVH GRWNYIRTCK YTVGTFWKEL LFYLTQALYQ RSVGYTGTSL
YESWSLSMFN TLFTSLPVIF MGVFEKDLSA ATLLAVPELY VIGQVNGGFN VRVYLGWMFM
ASAEAMAVYF VPWGLFGHVP FVEDGGIYAL GMIVYSAVVV IVAGKMQFLA TATLTSTNAL
AIIASIGGWF LWNIILSLTY APTARIYYVR SAFLTRFTWP WWLTLLLTLF AIFMFEIAVA
AFMNTFAPSD EHVFRVLEKD AGIKRRFEEE AAQELQAGWQ RDKGGTKGDE EERVRAVVGM
LEERERARRE GEVVEILRNR GDGGEGDVTA AGVGGDEGAE ISRILSRGYG DVKAV
//
