ID A0A395NDD8_TRIAR Unreviewed; 1426 AA.
AC A0A395NDD8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=TARUN_8118 {ECO:0000313|EMBL:RFU74118.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU74118.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU74118.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU74118.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU74118.1}.
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DR EMBL; PXOA01000568; RFU74118.1; -; Genomic_DNA.
DR STRING; 490622.A0A395NDD8; -.
DR Proteomes; UP000266272; 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; 1.
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; 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:UP000266272};
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 378..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 422..445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1215..1237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1249..1266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1278..1304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1324..1344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 91..148
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1101..1350
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 161180 MW; EB72BB6CC157FAFF CRC64;
MAASLRGADG LKRSKSDEAS TLPGYPQSCA EAAIPATKTS VVQRIHDVAS TVYQKAIVEA
ILRRGELAAS KDGRHIPLRL ESDEPLIDTR RGQAYISNSI RTSRYTLWNF IPKQLFFQFT
RVGNFYFLCV GIPQMIPGLS TTGSYTTILP LLFFVCLTMF KEGYDDYRRH RLDKVENANF
ATILGKEDQY AARAARPARF IDRFNPFHAT TTNEPRPVPA DEFEGVRWVP TRWANIKVGD
VIRLTRDEPV PADIALLYSD GENNLAYVDT MALDGETNLK SKQVCHAIEG CDTIEGIAKC
AAEFVAEDPN PDLFNFNGKV TVNGKTLPLT LNEIVYRGSV LRNTTCAIGI VINTGEECKV
RMNSNRHPKA KKPALEKVVN RIVITLAFYV IILSVGVSMG YVRWQKSTER HSWYLNHASV
PFHEIIIAFI IMFNNVIPLS LYVSLEIVKI GQLLLLNSDI DMYDEESDTP ARCNTNTILE
NLGQVGYIFS DKTGTLTDNV MKFRKISVAG TVWLHEMDLD PQPQPDGSDS VSSIVKEVEF
PSRAPSVYRR DRLSVVIHED RPETLDSPMS PRQSMAGRRS SSQWRSTGRP DHVQPDVNTS
DLLEYMKQRP HSAFTRKTKE YLLAMALCHS CLPEHKDGKL DFQASSPDEL ALVRAAQEMG
YLVVQRNSKQ ITLQVTQADG TVESLNYDIL DIIEFSSARK RMSIVVRYPD GRISVICKGA
DSAILPRLRL SSLAMQKATE VRQSADLEHE MFRRSEQLEP RNSFGGRPSL SIRRNPTITR
ERSVHRQSMG NRSRSFELNK LTRRSEDRPR LTVNTRGVSF DIANRPYLSP MSPHAPAPLD
PRLTFLEDSG IFDESEVFTK CFKHLDDFAT EGLRTLLFAQ KFVSESEYRS WKKLYDDATT
SLTNRQDKIE AAGEMIEQSF ELVGGSAIED KLQKGVPETI DRLRRANIKI WMLTGDKRET
AINIAHSARI CRPGSDLYIL DITKGSLETQ LSAMAEDLHA GSIHSVVVID GQTLAAVEKS
DALSVQFFAI MLLVDSVICC RASPAQKALL VRTVRSKLKA YRGEKRRGLT LAIGDGANDL
AMIQASHVGI GISGKEGLQA ARVADYAIAQ FRFLQRLLLV HGRWNYVRTA KFIVCTFWKE
MFFYLPAAQY QRYNGYTGTS LYQSASLTVF NTLFTSLCTI CMGIWEQDLS AETLLAIPEL
YVYGQRNMGL NFWKYMRWMV LAAIEGVITW NGIWAGYGWV SPAAKDENLY AIGSLVFTVG
VLWINWKLFI FETHYKSAVV MACFFVTTFG WFAWLAFLDG VYGATPSGVY DIRRTFSKLW
GGDAVWWSTA FIVLSFMGMI ELLFKALKRG MLVAGLWHWP PWQKKRLGEN VEEWDLELWQ
EMEQDPTVKR KLAKMARDHD DLDIEEDDEE EDIMEQIEID ISAGRR
//
