ID A5DGU3_PICGU Unreviewed; 1633 AA.
AC A5DGU3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=PGUG_02494 {ECO:0000313|EMBL:EDK38396.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38396.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK38396.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408157; EDK38396.2; -; Genomic_DNA.
DR RefSeq; XP_001484765.1; XM_001484715.1.
DR STRING; 294746.A5DGU3; -.
DR GeneID; 5126828; -.
DR KEGG; pgu:PGUG_02494; -.
DR VEuPathDB; FungiDB:PGUG_02494; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; A5DGU3; -.
DR OMA; ITTSHYT; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000001997; 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 GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
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 NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 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 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:UP000001997};
KW Translocase {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 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 499..520
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 540..563
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1335..1355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1367..1384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1396..1421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1441..1461
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 191..249
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1221..1470
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 185320 MW; B457A67B185ABE85 CRC64;
MSFNGATSGD SLSLPVPANV KRKRGLSLRS QLLNKSLWTH TDINDDPKSN NRSSKNSDGS
IQNIELDVME ENSGPNTTPH INIIHDDEEL KDYQPYNTLN SNMSRSTTQL TYASSRSDLT
SIGSNTYLGP GPRYRRRNRF YKFIKRILGQ NDLQPTENGR IIPLSLNKSD ANSYFSQEFY
DTYNKSYLDE RSGEPYCSNL ITSSKYNIYT FLPLQLKAQF SKIANCYFMV VAIMQMIPSW
STTGKFTTIV PLLIFMSISI AREGFDDWKR HGHDKEENNK FTTIIEEDKD LSSFDTHSVT
TIMTETMQVP PLNSALRSNQ ITPVNSNEQE EMHYTRRQAM KRYNLKETKT PWKHLKVGDF
VKVREDEWFP ADVVLLSTSE KTNEAFVETM ALDGETNLKP KAPHPELESI YSSVPGLKNN
KSIITVEDPN TDLYNFEGRF QKDGTMYALG SDNVAYRGSI LRNTKSVIGV VIFTGEETKI
RMNNIKRPRT KAPKLQRNIN YIVIFMVFVV LMLSCFSMMA QRLMYDWHKV SDWYLFGQDA
GVAPTLMGFI IMYNTLIPLS LYVTMEIIKV MQLLFLQFDI DMYHAESNTP ADAKTATILE
ELGQVSFVFT DKTGTLTDNK MEFRKFSVCG ESWLHNLDLL ANQDAIEPSD HQPSSAERAR
TSMDVVSLNS HTSYRSTANP NENQEYKTSL QLLKHLQLNP NTIFSKKVKF FLLSIALCNT
CLPRSSATES SNSSRNSSME DISEIPTNNS DGSIEYQAAS PDELALVKAA RDLGYVVFDK
QANTLTIKTY PMGFENDARL ETYEVLNIVE FTSSRKRMSA IVRFPDQRIC LLCKGADNII
IEKLKNSQMV QQKAKEISQN SADRKIMEAD IVLQSRFSNE LESRKSLSSL RQRLSFDSLR
DGQERARTMN SIDNFLSNKD EGELTEVASQ HRKSLHNQQV KKYSLDMSRA NNEQTANTDS
STDNQAFSVP NDRLVLHEEY VAERTLQHIE EFSTEGLRTL MYSFKWLDEK EYETWADKYA
SAKTALTDRA ALVEEVGGEI EYDLELLGAT AIEDKLQDGV SEAIEKLRRA GIKLWMLTGD
KRETAINIGY SCRLIKDYST VVVLSNDEPR DTIVQRITSA TSEIQAGRVA HFVLVIDGAT
LGELESDSTI MTLFFELCVL ADSTICCRAS PSQKASMVSS VRDLNKRAVT LAIGDGANDI
AMIQSADIGV GITGKEGLQA ARSADYAIAQ FRFLLKLLLV HGRYNYVRTS KFVLCTFYKE
LLFYLTQALY QRNTLFSGSS LYESWSLSMF NTLFTSLPIL CIGMFDKDLK PATLIAVPEL
YAKGREYRAF NLRVFVAWMF LAAFQSVGIS FISWYIWGFT ALHDNSVLPL GTMMFAALTI
IINAKITLIE MQNRQWLAFA SFIISVGGYG LWNVLIMFLY RSKDSPIFFV AYGLLTFGSD
ASWWAGLLIL FTIPLLFDIF LKVFLFSVRP SDDQIFQVFE RNIDLRRLFE QKAIKELAPG
WTYPKESSIW RKWCVKGINR VRKVFNMDPL HIKEKEETLI SLNESTSQRK RAGTNPNPTE
LPPGSGGEAI RVADRDLDMS DYDILPSGKM VKIANSNPGM LSKIGRRFGS GENVDEIIAH
RLESLRKQEE GDY
//
