ID A0A4T0W4B0_9PEZI Unreviewed; 1500 AA.
AC A0A4T0W4B0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CH35J_006110 {ECO:0000313|EMBL:TIC99595.1};
OS Colletotrichum higginsianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=80884 {ECO:0000313|EMBL:TIC99595.1, ECO:0000313|Proteomes:UP000305883};
RN [1] {ECO:0000313|EMBL:TIC99595.1, ECO:0000313|Proteomes:UP000305883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TIC99595.1,
RC ECO:0000313|Proteomes:UP000305883};
RX PubMed=31028389; DOI=.1093/gbe/evz087;
RA Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA Shirasu K.;
RT "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT Pathogenic Fungus Colletotrichum higginsianum.";
RL Genome Biol. Evol. 11:1487-1500(2019).
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:TIC99595.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWPZ01000004; TIC99595.1; -; Genomic_DNA.
DR Proteomes; UP000305883; 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; 2.
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 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; PF00122; E1-E2_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:UP000305883};
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 489..511
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 531..552
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1256..1276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1306..1327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1339..1356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1368..1393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1413..1433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 213..271
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1192..1442
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..872
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 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1500 AA; 169174 MW; 08FDCDAA7CC9882E CRC64;
MDRRHPGDAP SRQHHEDEDP APSPLPSSLS FDDHGRDDSH DLPDPSVNLA HRPAQRIQPR
RAVTEPMGSK GALDGGHVRF SDELPRDAVR GFDPASSHPN LSNPGLYTIP SRGDLESHIT
PEPSSSRPRP NSDQSSAQPS DADLKYPVYR PEPTKRTKWR VAKESMSERF KKAYELYFLQ
GLLRQKPLPP SADGRHIPLD MSRSRSDALI DERTKKPYRS NFIRSSRYTI WSFLPKQLLF
QFSKMGNFYF LVVGIIQAIP GLSTTGQWTT IAPLAVFVSL SMAKEGYDDY RRYLLAKTEN
LSRTWVLGER SKKATARMKS RKGVELSEPS DEGWTEIEWQ DLKVGDVVKL RRDEDIPADI
VLLHATGPNG TAYIETMALD GETNLKAKRA ATILAERCQT VEGIKSCQAT IVSEDPNLDL
YRYDGRVTVK EETLPLSLDN VIYRGSTVRN TTEAIGIVVN TGEECKIRMN AHKHVRTKAP
AMQRVLNRIV IWLIFVLLAL SSGLTLGHYL WRDPVEEGAW YLMGDNISLR NIFIAFILMF
NTLIPLSLYI SLEIIKIIQF YMMGDVEMYD PVTNTPMVAN TTTILEDLGQ VNYVFSDKTG
TLTENVMRFR KMSVAGTAWL HDMDIERDEQ AKQKLIEMAR KKRKGKGKDK NRDRAAGDND
ANPFQLQPAQ RRQSLSSYGR GRSASRAPQD EPELKTEDLL DYLRRKPDSA FSKKAKQFLL
CIALCHTCLP EVKEDGGIEY QAASPDELAL VEAARDLGYL LIDRPAQSVI LQLPGADGTV
EKETYQVLDV IEFSSQRKRM SIIIRMPDGK VCVFCKGADN VILPRLKLSG LALQKANDVN
RRASVRRSIE REKAQQRLST SGTPRSSFML GRTSMSDRRN MMNQRISGDM YRRSSVVHDG
PEEWSPRRGS ADVVSSASVH DMWASPRHSM AMSATEAEVD EFVDETIALN EGTVLERCFQ
HINDFASEGL RTLLYGYRYI SEDDYNSWRK IYQAATTSLD NRQEKIEAAG ELIEDKFDLA
GATAIEDRLQ EGVPDTIDKL RRAGIKVWML TGDKRETAIN IGHSAGLCKP FSEVFILDAT
MGNLRESILS TLGEVARGMA PHSVVVVDGQ TLGVIEGDED LSFLFFDLVV RVDSVICCRA
SPSQKASLVK RIRRQVPHSL TLAIGDGAND IGMIQASHVG IGISGREGLQ AARISDYAIA
QFRFLQRLLF VHGRWNYLRT GKYILATFWK EVVFFLPQAY FQRYTGYTGT SLYENWSLTV
FNTFFTSLAV ILLGGLEKDL QAKTLLEFPE LYTYGHKNRA FNVKLYIGWT FLGLIESLVI
FWVTWAVYNS LPFDQDTSLY AMGTVPFTVC VVFINIKLMV LEMENKNIII LIGFLLSVGG
WFLWNIILSA AFQNVMRIYQ IRHAFLQNFG RTLSFWTTIL LALAAVICLE LVVDAIRRVY
WPRDVDLMQR LERKGLNEND RETGQGDASG TVLEVVGDKT FKDVEGGVWP QVFHTPGWKG
//
