ID A0A4U0UQF4_9PEZI Unreviewed; 1235 AA.
AC A0A4U0UQF4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B0A54_11104 {ECO:0000313|EMBL:TKA38090.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA38090.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA38090.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA38090.1,
RC ECO:0000313|Proteomes:UP000310066};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:TKA38090.1}.
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DR EMBL; NAJP01000047; TKA38090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0UQF4; -.
DR STRING; 329885.A0A4U0UQF4; -.
DR Proteomes; UP000310066; 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; 2.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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 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:UP000310066};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1076..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1106..1122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1153..1171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 930..1178
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 434..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 138303 MW; 8F47734EA99A5F59 CRC64;
MANKDNSLST TGSYTTILPL TFFLLLTICK EGWDDMKRHK MDKVENNQYA TVLRKRQAAV
DGVASSRGLA RTLSLSGMLP WASKMANDVV DEVLEGDEDV NLQWAKVRWR DMKVGDIVKL
RRDEAVPADL ALLYADGEDG IAYVETMALD GETNLKSKQA PRGLRTCSNI SGIKKCAADF
VCEDPNRNLY DFNGRVTIDD ITIPLTLSEV LYRGTTLRNT THAIGLVLNT GEECRIRMNS
HNRPAAKKPR LERYANQVVL FLIGYVVILS VGVSVGYVIW HQHLEVRAWY LNNAYVDFGQ
IIVGFLIMFN NVIPLSLFVS LEIVKIGQMI LVHNDKEMYD EETNTPMVCN TNTILENLGQ
VSYVLSDKTG TLTENIMKFR GMSVAGLAIT HGTEPTCRDD SLDVRRTSEC TPPEKDLTGL
VGEKKVSITV ERRDVAPVET GARQHGRPSL QQRPSSDVPR RSVPGTDSFV STAELIRYIT
DHPSAAISLK ARDLILAMAL CHTALPETTK DGTINFQASS PDELALLEAA QDLGYLMISR
SSHSITLLRS GADGQQSREL YEVLDVIEFS SQRKRMSIIV RCPDGRIWLL CKGADSVIVP
RLQQAALASR KSHEVRRSLQ AEREQLRRSE QMTPRNSFGA MPSMTSRRRG SMEIRRDPAV
EHARLEVPGG ERTGKPYLRR LQGFAVADDA TVFSRCFKHM DDFAIQGLRT LLFAHKTISP
SEYAGWKKLY QDATTSLTGR QERIEATADM IEQGFDLLGA SAIEDKLQKG VPETIEKLRR
ANIKIWMLTG DKRETAINIA HSAQICKPES DLFVLDSAKG GLEAQLRDAA MLYRDAIDIH
SVLVIDGHTL SQVDAEQDLK QIFYNLIPLV DSVICCRASP SQKAGIVKAI RSRIPSALTL
AIGDGANDIA MIQACHVGVG ISGKEGLQAA RVADYSISQF RFLQRLLLVH GRWNYVRTAK
FITWTLWKEF WFYLMQALYQ HHNGYTGTSL YENASLTVLN TLFTSLCVIV PGIFEQDLKA
ETLLAVPELY VYGQKNKGLN LPYYLQWVLL AVSESMIVWF LTWASYGHFA QMSDNGLFAL
GNLLFTEGVV FTNYKLLVLE THYKTVIVGV SFLITVGGWW AWQGFLSHAY STNISPYDVK
GGFTSTFGND PNWWLTLIVV LAVLTVMELG YKSIKQSLLV AGLWPVWRLF GGRARRDADE
LDVGLWQAME KEPEMRERFM RMNDVHEGDD EDDCG
//
