ID A0A5N5P7R9_9PEZI Unreviewed; 1741 AA.
AC A0A5N5P7R9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=GE09DRAFT_596659 {ECO:0000313|EMBL:KAB5575564.1};
OS Coniochaeta sp. 2T2.1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5575564.1, ECO:0000313|Proteomes:UP000325492};
RN [1] {ECO:0000313|EMBL:KAB5575564.1, ECO:0000313|Proteomes:UP000325492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5575564.1,
RC ECO:0000313|Proteomes:UP000325492};
RX PubMed=31572496;
RA Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT 2T2.1 and its exceptional lignocellulolytic machinery.";
RL Biotechnol. Biofuels 12:229-229(2019).
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:KAB5575564.1}.
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DR EMBL; VSMA01000005; KAB5575564.1; -; Genomic_DNA.
DR Proteomes; UP000325492; 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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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; 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:UP000325492};
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 565..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1357..1377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1407..1426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1438..1457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1469..1494
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1514..1534
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 267..324
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1293..1543
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1665..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1689..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1741 AA; 193181 MW; 8D6D7FE2381286B8 CRC64;
MAPKDQPDAA EALRNQLEHV EEQQQDMEVP VSPDSRRASR LSTMDDAQAL SRTTSPVLTR
NGSRHRLSQE GPSRVRFSDD SPDARRRSLA IDPPRRQYPS NLHLDTEPVA LYTIESNVEH
RGRPRGQTLE QPVVLEQDET SPSRRADPRA SSVSGYYSLN SPATGAPPPS QHTEGFAAGL
KGAVVTAAET NVRLANYRDW LAKQKKRQRR WTSGPTGRLK ATSAALYKRF ILEVLLRQKP
LPPSVDGRHI PLNPGLSRRK PLVDERRGKP YVSNFIRSSR YTVWDFLPKQ LFFQFSKLAN
FYFLLIGILQ MIPGLSTTGT YTTIGPLMAF VALSMGKEGY DDYRRYKLDK LENRSETWVL
DPEGSVKRRS RRGGGGGGIL KNLFTRAKAV VGDEMTELEG VTSAPRDSSW SRVLWQDVRV
GDIIRLRRDD NIPADIVLLH ATGPNGVAYI ETMALDGETN LKSKYASPLF AGKCATPAGM
ASCDATVVSE DPNLDLYNYE GRVTVNGETL PLTLNQVVYR GSTLRNTDEA IGLVVNSGEE
CKIRMNATKN VRAKAPAMQY KVNRIVFLLV IFVVLLSAGC TIGNEIWKDQ YAPKAWYLEG
DKVPTKEIIV GFIIMFNTLI PLSLYVSLEI IKIGQLLLMQ DVEMYDPDSD TPMVANTTTI
LENLGQVSYV FSDKTGTLTE NVMRFRKMSV AGTAWLHDMD LQRDAVEKER KRMTMDIKRG
KSMDTKRGKS KAKHSMEASV ARKSMAADDG AAAERSPIGG GHPGLARRGS SFSQWKSSVR
PTHAQPELKT EDLIAYIRAK PHTPFSRRAR HFILCIALCH TCLPEIGEDG DTTYQAASPD
ELALVDAAKD LGYLVIDRPA QSIKLQFRDI DGSTVTESYE VLDVIEFSSK RKRMSIIIRM
PDGRTCIFTK GADSAILPRL QLNNLAAQKA SAVERRATQR KSVEQEKALQ RRSMQMVNRN
SLKLGRAAQQ MSLRKSKDKR SASLVRRTSL VTDEVDSWLN CRETEDFDEP IGNADAYVVP
RRSIGGGRSL DYTSPIADPY DGLVDESLAT QDGAIFERCF QHIDDFASEG LRTLLFAYRY
LEDDEYKKWK TIYHDATTSL VNRQDRVEAA AELIEQGFDL AGATAIEDKL QQGVPDTIDK
LRRANIKVWM LTGDKRETAI NIAQSARLCK PFSEVYILDA TQDRLQEKIA STLIDVGRGM
IPHSVVVIDG HTLSVVEEDE SVKILFFDLA ARVDSVICCR ASPSQKATLV KCIRDRVPSS
MTLAIGDGAN DIAMIQASHV GIGISGKEGL QAARISDYSI AQFRFLQRLL FVHGRWNYIR
TGRYILGTFW KEIVFYLVQA QYQRYNGYTG TSLYESASLA VFNTLFTSLP VILLGIFEQD
LSAETLLAVP ELYTFGQKNL GFNFRKYLVW MFMAATESIL IFYAIYGIYT SALFTDDTTL
YAIGTLAFSV CVIFINIKML VLELHNQTVI TLVGLLISVG GWFVWNLFLS AIYSPKPGPY
AVRDAFTHNF GRSPVWWLTG LMALVAVIVF ELLVASVRRA YWPRDQDLMQ ALEKDKGIMQ
VMREHAAERG EAAEGVSPNQ AMGLSSLPAK PLDSTTSPTD TPLPTPGGGG VTEVPGWGWH
RPSDPLTPSA VTPSADVTSK RNSRNLVLPP EKNTAVVAVA AAAAEAEARE NPTPLPPTTR
PAAVRRSSAE PTRSGSWLAA TAEMSGANSG AGGERGSGGY FVQSPIEMRM PSIDERRRDE
V
//
