ID A0A5Q4C007_9PEZI Unreviewed; 1322 AA.
AC A0A5Q4C007;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=NEO1 {ECO:0000313|EMBL:TQN72675.1};
GN ORFNames=CSHISOI_02797 {ECO:0000313|EMBL:TQN72675.1};
OS Colletotrichum shisoi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=2078593 {ECO:0000313|EMBL:TQN72675.1, ECO:0000313|Proteomes:UP000326340};
RN [1] {ECO:0000313|EMBL:TQN72675.1, ECO:0000313|Proteomes:UP000326340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2018a {ECO:0000313|EMBL:TQN72675.1,
RC ECO:0000313|Proteomes:UP000326340};
RX PubMed=31527702;
RA Gan P., Tsushima A., Hiroyama R., Narusaka M., Takano Y., Narusaka Y.,
RA Kawaradani M., Damm U., Shirasu K.;
RT "Colletotrichum shisoi sp. nov., an anthracnose pathogen of Perilla
RT frutescens in Japan: molecular phylogenetic, morphological and genomic
RT evidence.";
RL Sci. Rep. 9:13349-13349(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:TQN72675.1}.
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DR EMBL; PUHP01000153; TQN72675.1; -; Genomic_DNA.
DR Proteomes; UP000326340; 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; 1.
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; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
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 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:UP000326340};
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 202..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 561..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1116..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1149..1168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1252..1272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1278..1304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 188..241
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1086..1313
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 145877 MW; BEC59FBFB4AFD0DC CRC64;
MPSQTSYRSA DPPGSPGNDS DSDLDLDIQE LDPATTTTKR SSGLIRHDRQ STEHRSPRIA
LRNLRMGGSR RAGQKARGYG ELGQNRDDAS EDAQALLGEP GGSSSSSSRY RDGNPGAGSD
DDSPLLPGGS PPRRRSFAGD RFERLTSSLR LPSFMSNSGT QEAAKDDGQD QDEDDPSSSR
LVAVGSSQAT RFPPNLISNA KYTALTFLPV TLYNEFSFFF NMYFLLVALS QAIPALRIGY
LTTYVAPLAF VLVITMGKEA YDDIERRRRD NEANAEAYTV LVFEEPGRGM VSGQRSHKRL
KSDSLRKKGK NTVNIRDRLS DIREEEERAE GDGPVAEPSS FVREVGRKSR DLKVGDVLKL
SKGQRVPADV VILKCITSET TNASPVMETI VEEESLLVNT DEEPGNVKLP TKGKEVESND
NAGGATGETF IRTDQLDGET DWKLRLASPL SQTLPAEEFV RLRVTGGKPD RKVNEFLGTV
ELLPSRRDAQ DQQGALEGDD GTSAPLSIDN TAWANTVIAS NATTLAVIMY TGPQTRSALS
TAPSRSKTGL LEYEINSLTK ILCALTLALS IILVALEGFG NTEGNVWYIK IMRFLILFST
IVPISLRVNL DMGKSAYSWF IQRDPGIPGA VVRTSTIPED LGRIEYLLSD KTGTLTQNEM
EMKKIHVGTV SYANEAMDEV TSYVKQGFHI QPTTDPSSHT MLITPSSTFA NSTNVGATRT
RREIGSRVRD VVLALALCHN VTPTTEEEDG KTVVSYQASS PDEIAIVRWT ESVGLRLAYR
DRTSMVLEST ENGREIVRVR ILDVFPFTSE GKRMGIVVQF LEQARSTAPN LADSEIWFYQ
KGADTVMSPI VAENDWLDEE TSNMAREGLR TLVVGRKRLS YEQYKEFTGS YQAASLAIAG
RDAGMQRVVA QHLERDLELL GVTGVEDKLQ KDVKPSLELL RNAGIKIWML TGDKVETARC
VAVSSKLVAR GQYIYTVSKL KKKDNAQDHL DFLRGKTDSC LLIDGESLAL FLTHFRIEFV
SVAVQLPTVV ACRCSPTQKA EIAKLIKEYT KKRVCCIGDG GNDVSMIQAA DVGVGIVGKE
GRQASLAADF SIEQFFHLTK LLVWHGRNSY KRSAKLAQFV IHRGLIIAVC QTMYSIAIKF
EPEGLYKNWL LVGYSTVYTA FPVLSLVLDK DVDENLANLY PELYKELTSG RSLSYRTFFV
WVAVSIYQGC TIQGLSQILT EVEGPKMVAV SYTVLVLNEL LMVAIEITTW HPVMIISIVG
TFVVFVGSVP FLGDYFDLQF IITLGFIWRV LAIAAISLIP PYAVKLIRRT MKPPSYRKVQ
ST
//
