GenomeNet

Database: UniProt
Entry: A0A0A1TCK4_9HYPO
LinkDB: A0A0A1TCK4_9HYPO
Original site: A0A0A1TCK4_9HYPO 
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
//
DBGET integrated database retrieval system