ID A0A0D2G543_9EURO Unreviewed; 1545 AA.
AC A0A0D2G543;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Z518_00953 {ECO:0000313|EMBL:KIX09872.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX09872.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX09872.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX09872.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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; KN847475; KIX09872.1; -; Genomic_DNA.
DR RefSeq; XP_013277008.1; XM_013421554.1.
DR STRING; 1442369.A0A0D2G543; -.
DR GeneID; 25289024; -.
DR VEuPathDB; FungiDB:Z518_00953; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000053617; 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; 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; 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 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:UP000053617};
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 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 157..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 532..555
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 579..600
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1148..1167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1179..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1230..1251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1271..1289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1336..1356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 95..154
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1116..1365
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 174923 MW; 6F1DAD67952E568E CRC64;
MARIHFTSGE SNVSRPVRRM RWATTRKPGQ SGAKKRMSLL QRMPRVTVSS YEEKATGHKN
NGETSEESPM DEQKPEKGSQ ERTIYVNQPL PPEAKTEEGH IKAQYARNKI RTSKYTPLSF
VPKNLWFQFH NIANVYFLFI AILSIFSIFG ASNPGLAAVP LIFILTVTAI KDAVEDWRRT
VLDTELNNSP VYRLVDWDNV NSSDDDISLW RRFKKACTRL VISTYRWLKN SKRRKSKRSE
KDPTALGLQR SPSTATRATI RSSIYSEHTS FHSTHSQTGD DIAMTPVPSP AYRSSLSPNG
QLSANGEPPS SALSYETADE AGAGADNAPS MLRVQDPAKR KSNVPAPKDY GSFINPHKEV
PDKARFKKDY WKNVKVGDFV RIYNDEQAPA DVIVLSTSDP DGACYIETKN LDGETNLKVR
QALQAGRKVR HAKDCEYAEF VIESEGPHPN LYSYSGVAKW RQQDPKDPNG TPREMAEPVT
INNMLLRGCS LKNTEWVLGI VVFTGGETKI MLNAGITPSK RARMARDLNW NVIYNFIILF
FMCLVAGIVQ GVTWAEGNNS LDYFEFGSIG GNPPTDGFIT FWSAVILFQN LVPISLYITL
EIVRSIQAFF IWSDVHMYYE RLDYPCTPKT WNISDDLGQI EYIFSDKTGT LTQNVMEFKK
CTINGVPYGE AYTEAEAGMR RRQGVDVEAE AARVHQEIAE ARVEMLRLLR KTHDNPYLHD
DELTFVAPNF VADLNGKSGE AQARANEEFM VALALCHTVI TETTPGDPPK IEFKAQSPDE
AALVATARDV GFTVLGRTKE DLHVNVRGED RTYHILNTLE FNSTRKRMSA IVRMPDGKIK
LFCKGADSMI YSRLARGQQQ ELRKATAENL EMFAREGLRT LCVAEREIDE DYYQEWNKDH
DFAAQALTDR EDRLEEVADR IERELTLLGG TAIEDRLQDG VPDTIALLGQ AGIKLWVLTG
DKVETAINIG FSCNLLSNEM DLILFDMPES KIEDASVLLD QHLRTFGLTG SDEELAAARH
IHEPPPPTHA LIIDGESLKL VLQDELRQRF LLLCKQCKSV LCCRVSPAQK AAVVQLVRNG
LDVMALSIGD GANDVAMIQE ADVGVGIAGE EGRQAVMSSD YAIGQFRFLQ RLVLVHGRWS
YRRLAESIAN FFYKNLVWTF ALFWYQIYND FDITYLFDYT YILLVNLVFT SVPVGLMGIL
DQDVSDKVSL AVPQLYRRGM ERKEWTQTKF WLYMADGLYQ SAICYFMGYL LFKPATFETE
NGRGIADRSR MGVYIACVAI IVINSYILLN TYKWDWIMML VTVISCLLIF AWTGIYSSFE
SSFQFYKSAA EVYGQLSFWA YLLLTIIICL LPRFSIKYFQ KNYVPYDIDI VREQVRQGKF
KYLDEYEAYV PPKLVDVSGT SSEQPEETPT EADGRGHGRY SSMAESQRPI YPPSEAPTRD
YRQPHSQTGS DGTDRTKPSL DMTRQPGESS TPEKAKRRRP TLERVRSSFE RQRQSFDKLR
PSFEGSRDFT SAAMLARMES SYSHPGSPLS HTNTRRTHDI AEELP
//
