ID A0A5M6C9I2_9TREE Unreviewed; 1324 AA.
AC A0A5M6C9I2;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CI109_001265 {ECO:0000313|EMBL:KAA5530462.1};
OS Kwoniella shandongensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1734106 {ECO:0000313|EMBL:KAA5530462.1, ECO:0000313|Proteomes:UP000322225};
RN [1] {ECO:0000313|EMBL:KAA5530462.1, ECO:0000313|Proteomes:UP000322225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12478 {ECO:0000313|EMBL:KAA5530462.1,
RC ECO:0000313|Proteomes:UP000322225};
RA Cuomo C., Billmyre B., Heitman J.;
RT "The Genome Sequence of Kwoniella shandongensis CBS 12478.";
RL Submitted (AUG-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:KAA5530462.1}.
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DR EMBL; NQVO01000004; KAA5530462.1; -; Genomic_DNA.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000322225; 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; 2.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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:UP000322225};
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 272..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 480..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 529..551
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1032..1052
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1072..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1115..1138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1150..1168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1180..1203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1223..1242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 212..278
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1001..1252
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 148034 MW; FC16AF4B04C5A217 CRC64;
MPPQNNPFED LLGDSQPGQA ATRHHDPFED ADGPDLFSSD NAAPYGQGSR SGQGGQGRSG
QQGYALDPFF DDDDEYGHPG QSSGYLAPQS SSTVNVAGRF GRSDPSMLES NMPLATSGAI
PAGFSGPIDD DDTKYHPSSS KGYGAGGDPF GDEDDGPSAY AFSAPGSGPY SKPRRGRWQQ
FREDHLTDVD WTFGVNALLG RRSKFDGVPR EISLNDPEGN RVQGFEGNSV TTGKYGPITF
LPKFLFAEFS RSANLFFLFT ACIQQVPNVS PTGHYTTIVP LAVVLIASAF KEIKEDLKRH
ASDRSLNNNE AQVLVNQQFQ PRPWKRIRVG DIVRLEANSF IPADMVLLSS SEPEGLCYIE
TANLDGETNL KIKQSHPSTA SLTNPQAASL LRGHLLSEAP NSSLYTYDGT FNLSSAHPGS
APTKIPVGPN QMLLRGAQLR NTEWVYGVVV NAGHETKLMR NATEAPIKRT AVERQVNRQI
LYLFVLLIIL SLISTVGSSI RTWFFSKQSW YLRLGNESEN KVKHFVEDIL TFIILYNNLI
PISLIMTMEV VKFQQASLIN SDLDMYYAPT DTPALCRTSS LVEELGQIEY IFSDKTGTLT
RNEMEFRECS IFGTMYAQTV DDSKREQGQK SFDTLRQRLL EDNEEAATIR EFLSLLAVCH
TVIPEEKEGK MVYQASSPDE AALVAGAELL GFRFHTRKPK SVYIDANGQP EEYEVLNVCE
FNSSRKRMST IVRGPDGRIK LYTKGADTVI YERLAPDQQF SEPTLVHLED YATEGLRTLC
LAYRDVSEEE YAKWSVMYDQ AASQMSGRAE ALDRAAEVIE QNLQLLGATA IEDKLQDGVP
DAIHTLQQAG IKIWVLTGDR QETAINIGLS CRLISESMNL VVINTETAVE TSELLNKRLF
AIKNQRLGGD VEELALIIDG KSLTFALEKD CADVFLELAV MCKAVICCRV SPLQKALVVK
LVKRSTDAPL LAIGDGANDV SMIQAAHVGV GISGVEGLQA ARSADVAISQ FRFLRKLLLV
HGSWSYQRLT KLILYSFYKN ITFALTLFWY SWFNDFSGQI SFEGWSMSYY NVVFTILPPL
VIGIFDQFVS ARMLDRYPQL YQLGQQNHFF TPVKFFYWVG NAFYHSVILF AFSCLVFYND
LLASDGKNSG LWVWGTTLYL AVLLTVLGKA ALISDVWTKY TLAAIPGSFV FTMIALPLYA
IIAPLLNFSI DYRGIVPRLW ADAVFYFVLL LFPIVCLLRD YVWKYYRRTY HPASYHIVQE
IQKFNLSDYR PRQEQFQKAI KKVRATQRMR RQRGFAFSQT ETSNQDQTRL IRAYDTSVAR
PTGY
//
