ID A0A2T6ZCW9_TUBBO Unreviewed; 1284 AA.
AC A0A2T6ZCW9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B9Z19DRAFT_1095310 {ECO:0000313|EMBL:PUU73319.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU73319.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU73319.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU73319.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) 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}.
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:PUU73319.1}.
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DR EMBL; NESQ01000388; PUU73319.1; -; Genomic_DNA.
DR STRING; 42251.A0A2T6ZCW9; -.
DR Proteomes; UP000244722; 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; 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; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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:UP000244722};
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 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1110..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1159..1183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1189..1207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1214..1234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1240..1266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 168..214
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1047..1275
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..296
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 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1284 AA; 139986 MW; 19C52E238804C770 CRC64;
MSSYIRVSSP SPSGESSDLD LDLEELDPTS GGGGVGSGGG AGYSVGYRSV LGENHRSSFS
PTRRGRTSVD GAGGPGRIAL RRMKGREGPE DEEALLGRRS REEDIHDEEE TSNLRDGGVA
GGGEMRLLRR LGSRISLRST TGEDAVVDFT PSKETRVVGL RPGGAGGKYP PNIISNHKFT
AFTFLPLTLW HEFSFFFNLY FLLVALSQCI PVLRIGFLSS YIVPLVFVLS ITLGKEAHDD
IARRRRDTEA NSEPYEVLSF TDGGVLKRKK GARLGKKKSA TGAEGQELRE GGDDSDDIRI
VSKKSKDLKV GDILVLKKDD RVPADVVILK TISNEVNQAE EGGGNDTSGE AFIRTDQLDG
ETDWKLRLAP ALTQALHCSS LAYLTITASA PSKEVNNFIG SISFNPSAPS STAPSAMGSS
MPLGPGASSS SLSALPATAS SSMGLSVDNT AWANTVLASN STTLAAIVYT GPETRAALST
SRSRSKTGLL EKEINNLTKI LCVLTFSLSI ALVALQGFES GQNEPGVKDS PNPGEVVSGS
WYIKILRFLV LFSSIIPISL RVNLDMGKSA YAWFIEHDKG IEGTVVRTST IPEELGRVEY
LLSDKTGTLT QNDMELKKIH VGTVSYAGEA MDEVADYIRL GFSTGGGKDA SGGVQAPPAI
QLNAATTRTR REIGSRVRDV VLALALCHNV TPTTTTDEGA SEATITYQAS SPDEIAIVRW
TESVGLRLSH RDRKGMKLQS VDTGEVVVRV KILEVFPFTS EGKRMGIVVQ FMAGEKSKEP
DLLGSGAEEE NSSTGDIWFY QKGADTVMSS IVQANDWLDE ECSNMAREGL RTLVVGRKKL
SIQRYQEFSA KHKAASLLLA NRDKEMGKVV EEYLEHDLEL LGVTGVEDKL QKDVKPSLEL
LRNAGIKIWM LTGDKVETAR CVAVSAKLVS RGQYVHTIAK LKRKDHAYDA LEFLRNKTDS
CLLIDGESLA LFLDTYKSEF ISLAVQLPAV IACRCTPTQK ADVARLIRVF TKKRICCIGD
GGNDVSMIQA ADVGVGIVGK EGRQASLAAD FSIEQFCHLT KLLVWHGRNS YKRSAKLAQF
VMHRGLVISV CQTMFSIASR GEPIALYQGW LLVGYASLYT MAPVFSLVLD RDVDERLANL
YPELYKELTE GRSLSYRTFF VWVLVSIYQG GIIQGLSQIL VGLDHFERMV SVSFTVLVLN
ELIMVALEIT TWHMWMIFAE LGTALFFFAS IPLLGEYFDL QYVISWAFVW RVAAISAISL
VPPWVVKTVR RRLKPPSYAK IQGV
//
