ID A0A0E9NGG6_SAICN Unreviewed; 1352 AA.
AC A0A0E9NGG6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=G7K_2965-t1 {ECO:0000313|EMBL:GAO48796.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO48796.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO48796.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO48796.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO48796.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO48796.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
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:GAO48796.1}.
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DR EMBL; BACD03000017; GAO48796.1; -; Genomic_DNA.
DR RefSeq; XP_019024730.1; XM_019166539.1.
DR STRING; 698492.A0A0E9NGG6; -.
DR GeneID; 30183386; -.
DR OMA; MHSFWSW; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000033140; 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:SF214; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000033140};
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 493..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 535..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1093..1115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1136..1160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1172..1189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1201..1224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1244..1263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 230..296
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1022..1274
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 21..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 817..844
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 29..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1352 AA; 151555 MW; CB25D598983A9134 CRC64;
MSWHPVEESR LDNDSLLDLN VDIGAGNPSN PGARQTTANP FTSQTSFDDF TNVGTSHGGG
GLSPQDPFAT PGRGAQTPMG QNPNPFLGYE DDLLDDDLEP VYGNAGQRAA DGDVRAYGDM
EVDDATGPGG VYGTLRGAVN KLTGGYAMQN DSDMDIPLTN ARAPTGMSMA RNADTLSLES
AEGIAMGEMG PGLTRERARP KATWKERVES WGRNLGRRGP DPSTLGPRII HLNDAPANNV
NKYVDNHIST AKYNLATFVP KFLFEQFSKY ANLFFLFTAI IQQVPTVSPT NRWTTIAPLA
FVLLVSAFKE LVEDVKRHQQ DRELNRSRAS VLEGNTFVDR RWVNVRIGDM VKVESEEYFP
ADLVLISSSE PEGLCYIETA NLDGETNLKI KQSLPETADL VSPAQVGSLV GRIESEQPNN
SLYTYEATLN LQSGGQDRKI ALGPDQLLLR GAQLRNTPWI YGIVVFTGHE TKLMRNATAT
PIKRTAVEKM VNIQIVFLFS ILIVLSLVSS IGSTVKEFVH GDSLSYLELA GVNQVGSFFL
DILTFWILYS NLVPISLFVT IELVKYYQAF LIDSDLDMYH EETDTPAVCR TSSLVEELGQ
IGFIFSDKTG TLTCNVMEFK QASIGGIPYT DVVPEDRRPA PGDTTDQNAL YDFDALQTNL
KTHETSEILD HFLTLLATCH TVIPERKADS DEIKYQAASP DEGALVDGAR KLGYKFVTRR
PRSVCVEVNG EEREYEVLNI NEFNSTRKRM SAVLRCPDGK IRLYIKGADT VINDRLGPNQ
VFKEITEQHM EEYATEGLRT LCLAMREVPE SEYLSWARDY DKAATSLDNR AEKLEAAAER
IEKDLFLLGA TAIEDRLQDG VPDTIHTLQT AGIKVWVLTG DRQETAINIG MSCKLISEDM
SLIVINEESF AGTQEHMQKK LSQLQSHADG ELESLALVID GKSLTYALEK DLEKTFFDLT
MMCKAVICCR VSPLQKALVV KLVKRHTKSL LLAIGDGAND VSMIQAAHVG VGISGMEGLQ
AARSADVAIA QFRYLRKLLL VHGAWSYQRL SKLILYSFYK NIALYMTQFW YAFQNGFSGQ
VIYESWTISF YNIFFTALPP IVIGICDQFI SARLLDRYPQ LYKLGIDGTF FNVRSFWSWV
GNGFYHSLVL YLCSIVIFRW DFQEADGEIG GHWVWGTSLF TAVLATVLGK AALVSDLWTK
YTYIAIPGSF LLWLGFLPVY AIVAPALNFS KEYKGIIPHL YGSWVFYVTW IVLPTFCLLR
DFVWKYYKRM YAPEKYHYIQ EIQKFNVADY RPRMEQFQKA IRKVRQVQRM RKQRGYAFSQ
ADEGQARLIR AYDTTRQRGR YGELREAQGN GH
//
