ID A0A1W2TLQ6_ROSNE Unreviewed; 1354 AA.
AC A0A1W2TLQ6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=SAMD00023353_1200100 {ECO:0000313|EMBL:GAP89260.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP89260.1};
RN [1] {ECO:0000313|EMBL:GAP89260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP89260.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; DF977457; GAP89260.1; -; Genomic_DNA.
DR STRING; 77044.A0A1W2TLQ6; -.
DR OMA; MHSFWSW; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000054516; 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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 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 SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:GAP89260.1};
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:UP000054516};
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 488..510
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 541..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1094..1116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1137..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1174..1194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1206..1227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1247..1268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 224..290
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1023..1274
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 906..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 39..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 151372 MW; 246AB97BF26EADAE CRC64;
MAGRKPLGGS SDSRNDLLLD LDDQPTYGGQ RAPVNDDELL RSYNTNNPGN EFPSRQSVSY
DDFIGASQTT HPSVKNPAAG ARASGIRPPY IPENDRQYSQ GSDLNNYRRY ADDFDDYPED
DQSFYQHGGE SMGGRDTTGR DIARNRNSVL GLGGGLLGRA KNMLGMGQGY SEMDLPLTDA
RHGRSDSSAT SPQAKQSKKF ELKSFKFGFG GGKPDPSTLG PRIIHLNNPP ANAANKYVDN
HVSTAKYNVA TFLPKFLIEQ FSKFANVFFL FTAGLQQIPG LSPTNQYTTI GPLIVVLFIS
AAKELVEDYR RKQADSALNN SKARVLRGSS FEETMWINVA VGDIVRVESE EPFPADMVLL
ASSEPEGLCY IETANLDGET NLKIKQGLPE TSALVSPSEL SRLGGRIRSE QPNSSLYTYE
AALTMQAGGG EKELPLNPEQ LLLRGATLRN TPWIHGIVVF TGHETKLMRN ATATPIKRTK
VERQLNKLVL ALIGLLLLLS SICTIGDLVY RAVRNDSVSY LELDDLNGAG KVVQAIFKDL
VTYWVLFSSL VPISLFVTIE LVKYWHGILI NDDLDIYYDQ TNTPANCRTS SLVEELGMVG
FVFSDKTGTL TCNMMEFKQC SIGGIQYAEE VPEDRRATVE DGVEVGIHDF KQLAENLRSH
HTSEAIHHFL ALLSTCHTVI PERDEKQGGK IKYQAASPDE GALVQGAVSM GYAFIARKPR
TVIIEVGGRE LEYELLAVCE FNSTRKRMST IYRCPDGKIR LYCKGADTVI LERLNDDNPH
VEQSLLHLEE YAAEGLRTLC LAMREVPEQE FQEWRAMFEK AQTTVGGNRA DELDKAAEII
ERDLYLLGAT AIEDRLQDGV PETIHTLQEA NIKVWVLTGD RQETAINIGM SSKLLSEDMM
LLIVNEEDAA ATRQNIEKKL EAIRNNAEGS IEMDTLALVI DGKSLTYALE PDLEKLFFDL
AVMCKAVICC RVSPLQKALV VKLVKKFSDE ILLAIGDGAN DVSMIQAAHI GVGISGVEGL
QAARSADVSI AQFRFLRKLT LVHGAWSYHR ISKTILFSFY KNIALYQTQF WYAFQNVFSG
EIIYESWMLS FYNVFFTVLP PLAIGILDQY VSARLLDRYP QLYAAGQRNE FFKIKTFSAW
IANAFYHSLI LYIFSELIWH GDGVLRDGTI GGHWLWGTGL YASVLTTVLG KAALVTSNWT
KYHIIAIPGS LLFWFAFIAV YGTVAPMVNV STELRGIIPV LFTSPNFYIQ TIFLPLACLI
RDVAWKYVRR MYYPRSYHHI QEIQKYNIQD YRPRMEQFQK AIRKVRQVQR MRKQRGYAFS
QADESQTRVL NAYDTTKGRG RYGEMPASTA PQGR
//