ID A0A1B9HWS0_9TREE Unreviewed; 1566 AA.
AC A0A1B9HWS0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=I206_06633 {ECO:0000313|EMBL:OCF47727.1};
OS Kwoniella pini CBS 10737.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF47727.1, ECO:0000313|Proteomes:UP000094020};
RN [1] {ECO:0000313|EMBL:OCF47727.1, ECO:0000313|Proteomes:UP000094020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF47727.1,
RC ECO:0000313|Proteomes:UP000094020};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000094020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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; KV700116; OCF47727.1; -; Genomic_DNA.
DR RefSeq; XP_019008946.1; XM_019158333.1.
DR STRING; 1296096.A0A1B9HWS0; -.
DR GeneID; 30175002; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000094020; 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 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:SF153; 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:UP000094020};
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 99..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1061..1083
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1089..1110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1140..1162
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..1267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 72..125
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1026..1274
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1566 AA; 175248 MW; C860ABB222767522 CRC64;
MATTSTSKTP LVPRSKKHKP SWYRRNIARP MSKLNPARLF HTGKKTLTSR SIYINEELPP
DFYDKKGRLL KNKKYPSNQN VTSKYTIITF LPRNLFEQFR RVANIFFAAI NILQFFPKFS
TISPGLVILP LIIVLAITAV KDGYEDIKRH QADHRVNHSI VHTLGGQDYE NKNPMKPKEK
TFVPAIPLPK LKSRKAKKAA LLEENRETAQ ANEAPPVAEP RGQDNGLSRM RSQVSNWQDD
EEAADAPNEL GWHRTIWEDV KVGDFVKIYD GEQFPADILI CSTSEEEDVA YIETKNLDGE
TNLKSRNGVP GLSHLDSAEA CAHAHVRIDL DAPEVNMFRL NGAVVNMEEV DEEGQHPIHP
CTLETTLLRG CILKNTAWVI GIVIFTGADT KIIQNAGRTP SKRSKVERQM NPQVLLNLFL
LALIAMVCAI VDHVNEVNWN KEQAYWMLYA DTSGDNPNVN GIITFLNAFI TFQNIVPISL
YISIEFVRTV QAAFIYWDRN IKYIKNGVVT RTTARSWNLS DDLGQIQYIF SDKTGTLTQN
AMIFRQCSVG GKIYTGDGKP PSHPTLTHLH SEPHVKQTSP ASSDTDDTAQ DGGEKADDVK
VALPKEVLAT FHDDELDKDL AAHDTEQSRV LHGFFAVLGL CHTVLAAEPE PGVIEYKAQS
PDEAALVQSA ADVGFVFRGR DHNVLKMSTP FSDNPDEYEL LHVLEFNSAR KRMSVILRKL
DEDGRIFLLV KGADNVIFER LSKDNSQKEL RQKTDQDLQY FASEGLRTLC LAYRVLGDKE
YETWAKDYHN ATVALQDREQ QVEDVSSRIE QGLVLLGATA IEDKLQDGVP ETITDLKRAG
IKVWVATGDK LETAVAIGYT TNLLTQDSNL IVVREGRHSI QDQIREALDG FFGGNDVTRT
ISRASTSRPS HEAPHLARVN TGVRSLVGHD NGTRPGGFSL VIDGHALAHC FEDPETEDLL
LALSTQCNTV ICCRVSPLQK AQIVHLIKDN LGVMCLAIGD GANDVSMIQA ADVGIGISGE
EGLQAVNSSD YAIAQFRYLK RLLFVHGHWS YYRNSSMILN FFYKNIIGIG VLFWYMVFCG
WSTTYVFAYV YLLFWNVFWT IMPVLAIGLF DKDIDDETLM ALPELYKKGR EGAYFGIKIF
CYYLFEGFFQ TAVIYFFIHY TYITTSARGD GYDVYIYEMS TTMVMGAVMV ANLFTGLNID
SWTGWTYFGI LFGPVLIWLF TAIYSIIPPS SFYTGVYGND VFLFRSAAFW FGWPFVLVIS
LLPRYILRYL DQNAFGDDIA KMRLVRKYNP HVDPNTHPLL GGKLGEKDNK EDEDNSYGRP
QGQEENEDIR LQRLNSNVPP HELQEFGQDV EHGTQGRPSY ERNARNSFQS NRFGGHPQAR
GSAVDMSTGL SQEPSRGYGF TMEEGGVAIQ RMQSRLSQHS QNSNRYRLIP KMSSGSNNNK
VSISEPFGAP KGGGGSMAKI RERAGSILSI SRKRAGTDST HHSGGGGVSE SPHKSVGFLS
PSRRGSEKGK EDLNSPLSPS KRKQSKTQRD WTAQGHNARE GEGEEQSLGR DFGSGQNIAP
PEIPRV
//
