ID S0E5C9_GIBF5 Unreviewed; 1522 AA.
AC S0E5C9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=FFUJ_05901 {ECO:0000313|EMBL:CCT69971.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT69971.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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}.
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DR EMBL; HF679028; CCT69971.1; -; Genomic_DNA.
DR STRING; 1279085.S0E5C9; -.
DR EnsemblFungi; CCT69971; CCT69971; FFUJ_05901.
DR VEuPathDB; FungiDB:FFUJ_05901; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000016800; Chromosome 6.
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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000016800};
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 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 510..535
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 555..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1140..1156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1168..1189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1219..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1260..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1325..1345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 110..163
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1105..1354
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 877..904
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1522 AA; 171910 MW; B88DA85F76807F64 CRC64;
MTTTTTSDGH LDPQALSATQ RSRWATQRKS VNSSNNKRNS LLERMGHRKT GSNEKNPPSD
GSDPHGDDGQ PPQANPEDQN GGEEDEDHEN RTLFFNQPLP EELLDENGHP TQVFTRNKIR
TAKYTPLSFV PKNLWFQFHN VANIFFLFLV ILVIFPIFGG VNPGLNAVPL IFIIAVTAIK
DAIEDYRRTI LDIELNNAPV HRLRNWNNVN VMEGDVSMWR QFKKANSKFF GSIWRATQSL
WSKKAKEERA KRKASPAEDD APRPSVETHR TRQSMRQSIA SPFTGRESFM SAREDIQMTP
VPSPSPQATP AQFEMPDQQD AKRAAALSQM KSDVINYNHP PSGARFQKDT WKSLVVGDFV
RIYNDEELPA DVIILSTSDP DGGCYVETKN LDGETNLKVR QALRCGRGLK HARDCERAEF
VIESEGPQPN LYKYNGAIKW KQNVPGYLDE EPEDMTEPIT IDNLLLRGCN LRNTEWIVGV
VVYTGHDTKI MMNAGITPSK RARIAREMNF NVVCNFGILL IMCLLAAIIN GVAWAKTDAS
LHFFDFGSIG GKPAMSGFIT FWAAIILFQN LVPISLYITL EIVRTLQAIF IYSDVEMYYE
PIDQPCIPKS WNISDDVGQI EYIFSDKTGT LTQNVMEFKK ATINGQPYGE AYTEAQAGMQ
KRLGIDVEKE GERVRAEIAD AKVRALAGLR KIHDNPYLHD EALTFIAPDF VSDLAGESGP
EQQAANEYFM LALALCHTVM AEKVDGDKPK MIFKAQSPDE EALVATARDM GFTVLGSSGE
GINLNVMGQD RHYQILNTLE FNSSRKRMSS IVRMPDGRIV LFCKGADSII YSRLKRGEQK
ELRKTTAEHL EMFAREGLRT LCIAHKEVSE QDYRAWKKEH DAAASALEER EEKLESVAEL
IEQDLYLIGG TAIEDRLQDG VPDTIALLGN AGIKLWVLTG DKVETAINIG FSCNLLNNDM
ELIHLKVDED ETGEITDETF FDMAERLLDD NLQTFGITGS DHDLALAKKN HEPPAPTHGL
VIDGFTLRWV LNDRLKQKFL LLCKQCKSVL CCRVSPAQKA AVVAMVKNGL DVMTLSIGDG
ANDVAMIQEA DVGVGIAGVE GRQAAMSSDY AIAQFRFLQR LVLVHGRWSY RRLAESISNF
FYKNMVWTFS IFWYEIYCDM DMTYLFDYTY ILMFNLFFTS VPVAIMGVLD QDVSDKVSLA
VPQLYRRGIE RLEWTQLKFW LYMIDGVYQS IMVFFIPYLL FMPGTFLTGN GLGVEDRLRF
GAYVAHPAVI TINMYILINT YRWDWLMVLI VVISDVFIFF WTGVYTSFTS SAFFYGTAAQ
VYGEATFWAC FFLVPVICLF PRFAIKALQK VYWPYDVDII REQERMGKFA HLYQAEETSD
PLTADTKSDK SKSSKSSRRS KKMPKHVAYG SVDEDLRPIY PPSTATRTTT YNQHSQNGSD
STNYTAHRIS LDVPMQARPS IDRARPSYDR MRASMDRVRP SFEASNDFTS AARLSRIESS
QSQGGRFRPR LRGLSLTKSA NI
//
