ID A0A4V1XWT6_9PEZI Unreviewed; 1504 AA.
AC A0A4V1XWT6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=DL771_001174 {ECO:0000313|EMBL:RYP77379.1};
OS Monosporascus sp. 5C6A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211642 {ECO:0000313|EMBL:RYP77379.1, ECO:0000313|Proteomes:UP000292526};
RN [1] {ECO:0000313|EMBL:RYP77379.1, ECO:0000313|Proteomes:UP000292526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5C6A {ECO:0000313|EMBL:RYP77379.1,
RC ECO:0000313|Proteomes:UP000292526};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) 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:RYP77379.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QJOB01000012; RYP77379.1; -; Genomic_DNA.
DR STRING; 2211642.A0A4V1XWT6; -.
DR Proteomes; UP000292526; 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; 3.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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; 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:UP000292526};
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 485..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 521..544
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1266..1286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1316..1335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1355..1371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1378..1398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1404..1424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 184..242
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1203..1433
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1504 AA; 169521 MW; DDA25B7290766CAB CRC64;
MVSQEHGHGE SGASHSQQHL RVNTPSSNAG WANNDQQHSS GYAHVDIDRN PAQRGPPMQR
LHSAPASASA SSSIPDASRT ESEPDGYNHA SAKRPDSKKQ STDGENNGAF SDGSSPQLNN
YRAWVNRRQA KDHRTSLRQR FNTVYQKWVV EGLLRQKPLP PSKDGRHVPL IVRGARRKHL
IDERRGKRYI SNSIRSSRYT VWSFVPKQLI YQFSKLANFY FLVIGIMQLI PGLSTTGTYT
TIGPLLLFVA IAMAKEGYDD YRRYKLDKSE NRSLTWVLDP DGTIAKNRAV RKAKELAEKG
KGKSSRKQAD DGNEGAVTEL QEMGSRNNGE EGPWAEIEWR DVRVGDIIRL RRDDPVPADT
VLLHATGVNG IAYIETMALD GETNLKSKQA CPLLAKRCDT IEKMMNCNAT IVSEDPNVDL
YNYEGRVVLD GETMPLTLNE IVYRGSTLRN TKEATGLVVN TGEECKIRMN ANKNMRAKAP
RMQRFLNRIV LFLVLVLLCI TTGCTGGYYL WRRRYETGAP YLAGALVSFV EIWFGFIIMF
NTLIPLSLYV SLEIIKVGQY IFMHDVEMYD PETDTPLGIN TTTILEDLGQ VSYVFSDKTG
TLTENKMRFR KFSVAGSSWL HDPDVRRDEK EAELNSAAAE SQGSELPFHR TPTMNMIAEE
EEQSKTPAGS DRPLPRPFSG SSSTWGSPAQ PKQPQTEPNT MVLLDYIRTK PNTPFSRKAK
QFLLCMALCH TCLPEVRENG EITFQAASPD ELALVKAAQD MGYLLIDRPT QSIVLQIQNA
DGTLVKETYQ VLDVIEFSSA RKRMSIIIRL PDGRICIFCK GADNVILQRL KQSTLAMRAA
SEVERRASER RSMEADMVRR QRTSQSTPRN SMSLGFNQRQ GFMRRVNSVR KSTDLTRHSL
SISVPDEAGH QYPRSEIRRP DDEDAFQTTR HSMAVSPSSP RLGVDDHFPE PHIDESVAAN
DVAIFERCFK HVDDYASEGL RTLLYAYRYL SEADYTSWKK IYREATTSLV DRQRLIEEAG
EMIEKNLDLA GATAIEDRLQ EGVPETIEML RRANVQVWML TGDKRETAIN IAHSARICKP
YSEIFIIDVT LGDLQEKITS TLVDVGRGMI PHSVLVVDGQ TLSVIEQDDT LRIMFFDLVV
RVDSVVCCRA APVQKANLVK CIRKTVPKSV TLAIGDGAND IAMIQASHVG VGISGREGLQ
ASRVADFSIA QFRFLQRLLF VHGRWNYHRT GKYILATFWK EIVFYIVQAQ FQRSTGYTGT
SIYEKWNLTV FNIFFTSLPV ILLGIFEKDL SAETLLAVPE LYTYGQRNGG FNFQKYLGWM
LMGLAETVLI YWLSYAHWIR LTFEQDNSLF PFGQLVYQTC IVVINVKILI LELNHKVWIT
FVGFSLSIIA WFVWNVIIAS GYPVRWWVAS VGLIVAIITL ELGVTALRRI YLPSDTDLWQ
ELERLGQDSV RKVADEHTAA ELGQVLRAQV GDNPESPATE RKTEDTIKSE AAHDDRPVTG
RSFG
//
