ID A0A0A1TCK4_9HYPO Unreviewed; 1457 AA.
AC A0A0A1TCK4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=VHEMI03885 {ECO:0000313|EMBL:CEJ85734.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ85734.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ85734.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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 ---------------------------------------------------------------------------
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; CDHN01000002; CEJ85734.1; -; Genomic_DNA.
DR STRING; 1531966.A0A0A1TCK4; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000039046; 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; 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:UP000039046};
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 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 381..405
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 425..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1227..1249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1261..1282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1294..1315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1335..1355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 97..152
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1113..1362
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1429
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 164481 MW; F4C4DD1F72B91835 CRC64;
MQLETLPSLV SNPSGTEKQP PGHRRLAQDS KEPWTSKAKG LMNMHWQSRL ENAVSGVYEN
TLKPIFHKKR IEASAHGRRV PLNVENVEPL IDVRRGHAYI SNDIRTSRYT IFDFIPKQVL
FQFSRVGNFY FLCVGIPQTI PGLSTTGSFT TILPLLFFVL LTVIKEGYDD YRRHRLDKVE
NANFATALGR KDNYTGKLDT SRPRDKFNPF KSKLKAKPRP VPSDEYDGLK WVPKRWSELK
VGDVIHLSRD EPVPADIILL HSSGENGLAC IDTMALDGET NLKNKQVSKA LESCSSIEGL
ANCNAEFVVE NPNPELFNFD GHITVDGQSA PLTLNEVIYR GSVLRNTSHA TGIIYNTGEE
CKVRMNANQH PRAKKPALER VVNRIVITLA LYVVILSVGV SMGYIQWQKS YEQYSWYLDQ
ASVPFHEIII AFIIMFNNVV PLALYISLEI VKIGQLLFLN SDIEMYDEES DTPARCNTNT
ILENLGQVGY IFSDKTGTLT DNVMKFRKIS VAGTVWLHEM DFEQPDETAL STTEEIESVP
ATDMEDSSRE PSIYKPEPIR LTTPVTSPMK SPRSTIITET ALSPSRPSMG GRRSSSHWRS
TGRPDHVQPE VNTEDLLNFI RLRPHSAFAR KAKEYILAMA LCHTCLPETI DGKVEYQASS
PDELALVRAA RELGYIVATR TSQSISVDLM EADGTVQTQK FDVLDVIEFT STRKRMSIVV
RYPDGKISVI CKGADSAILP RLKLNSLAKQ KAHQVRMSAD VEHEKLRRSE QLEPRSSLGG
RNSLTIRHTP GVSKQPSGSR VSMLSRRKSF EVNKLMRRSE DTFAPMADRG GSFDISRQPM
RNTATTTVEP LPENLQFLEE QSVFDDSDIF TKCFKHLDDF ASEGLRTLLF AQKFMSEHEY
RAWKKVFDDA TTSIKNRKEL IEAAGDMIEQ SFELVGASAI EDKLQRGVPE TIDKLRRANI
KIWMLTGDKR ETAINIAHSA RLCKPGSDLY ILDVAKGDVQ FQLLALAEDL QAGSIHSVVV
IDGHTLSVVE KSPELSQQFF STMVHVDSVI CCRASPAQKA LLVRTVRSSL GGFREQRRRG
LTLAIGDGAN DLAMIQASHV GIGISGKEGL QAARVADYSI AQFRFLQRLL LVHGRWNYVR
TAKFILTTFW KEMFFYLPTA IYQKYNGYTG TSLYQDTSLT VFNTLFTSLC TICMGIWEQD
LSADTLLAMP ELYTYGQQNI GLNAWKYFRW MLLAAIEGVV AWYGVWAGYS WLQPAVRDQG
LYALGTLAFT VGILWINWKL FIFETHYKSS VVMWSFFITT IGWFAWLSFL DGVFAATSGP
YSIRGSFTKE FGLDVVWWAT LFGVLALLGL FEMILKTLKR ALQLSGLWQF PPWNSVGLSE
DLTQWDLELW QELEQNPAVR EQLKKMAQDE DDNDDDAGID LEEEEDVGRP NDNDSATPPS
HFAYLISRCR QMIPFRR
//