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Database: UniProt
Entry: A0A1W2TLQ6_ROSNE
LinkDB: A0A1W2TLQ6_ROSNE
Original site: A0A1W2TLQ6_ROSNE 
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
//
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