ID A0A168D573_CORFA Unreviewed; 1529 AA.
AC A0A168D573;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=ISF_01256 {ECO:0000313|EMBL:OAA72183.1};
OS Cordyceps fumosorosea (strain ARSEF 2679) (Isaria fumosorosea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=1081104 {ECO:0000313|EMBL:OAA72183.1, ECO:0000313|Proteomes:UP000076744};
RN [1] {ECO:0000313|EMBL:OAA72183.1, ECO:0000313|Proteomes:UP000076744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2679 {ECO:0000313|EMBL:OAA72183.1,
RC ECO:0000313|Proteomes:UP000076744};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA72183.1}.
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DR EMBL; AZHB01000002; OAA72183.1; -; Genomic_DNA.
DR RefSeq; XP_018707629.1; XM_018844863.1.
DR STRING; 1081104.A0A168D573; -.
DR GeneID; 30017548; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000076744; 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 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; SFLDS00003; Haloacid_Dehalogenase; 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:UP000076744};
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 148..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 515..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 560..585
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1145..1161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1173..1194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1224..1245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1265..1283
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1290..1310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1330..1350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 116..171
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1110..1359
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 258..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 882..909
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1529 AA; 172386 MW; F8B626DFF59E4415 CRC64;
MPDNLTPEGA AGNGADLDKV QTQRARWATR RMTVKSGSTK RHSLLNRHNR KKSSSSEKSV
GAPGGGDNGH GPLSNGDDNG DADDPEASET EDDEPENRHL YFNLPLPDDM LDEEGHPANS
YARNKIRTAK YTPLSFIPKN IWFQFHNVAN IFFLFVIILV IFPIFGSVNP GLSAVPLIVI
ICLTAIKDAI EDYRRTITDI ELNNAPVHRL MNWDNVNVEV GDVSTWRKVK KSTSRFFGGI
WYAVQSIWSK QARQKRIERK AKANGEEEEE PRPSVETQRT RMSMRRSITS PFGNRRSTHE
DIQMTPVPSP SPPGHIKIQE PDKQDQARLA AMQDMKTDII NYRRAPTNAR FKKDAWKNIV
VGDFVRIYND DELPADVIIL STSDPDGACY VETKNLDGET NLKVRQALRC SRALKHARDC
ERSEFLVESE APQSNLYKFN GAIKWKQTVP GYEDDEPEDM TEAITIDNLL LRGCNLRNTE
WILGVVVYTG HDTKIMMNTG MTPSKRARIA REMNFNVICN FGILFVMCLV SAIINGAAWA
RTDTSKNFFD FGSIGGSPPV TGFITFWAAI INFQNLVPIS LYITLEIVRT LQAIFIFSDV
EMYYEPIDQP CVPKTWNISD DVGQIEYIFS DKTGTLTQNV MEFKKATING HPYGEAYTEA
QAGMQKRAGI DVSSESERIH AEIAKAKADS IAGLRKMYDN PYFYDDALTF VAPDFVADLG
GESSKAQKEA NETFMLALAL CHSVIAEKAP GDTPRMLFKA QSPDEEALVA TARDMGFTVL
GSSGDGIDVN IMGEDRHYPI LNTIEFNSTR KRMSSIVKMP DGRIVIFCKG ADSVIYSRLK
KGEQRELRQE TAEHLEMFAR EGLRTLCIAM KEITEEEYRS WKKEHDVAAS ALEDREEKLE
AAAELIEQDF LLLGGTAIED RLQIGVPDTI ELLGQAGIKL WVLTGDKVET AINIGFSCNL
LNNDMELIHL KVDEEAGDDV SDDMLLDELE KGLDQHLSHF GITGSDEDLK AAKKNHEPPG
PTHGLVIDGF ALRWALHDRL KQKFLLLCKQ CRSVLCCRVS PAQKASVVAM VKNGLDVMTL
SIGDGANDVA MIQEADVGVG IAGLEGRQAA MSSDYAIGQF RFLQRLVLVH GRWSYRRLAE
SISNFFYKNM VWVFGLLWFQ IYCDFDITYL FEYSYIIMFN LFFTSVPVGV LGVLDQDVSD
KVSLAVPELY RTGIERLEWT QRKFWLYMFD GVYQSVMAFY VPYLIFSNSR PVTFNGLNVD
DRYRLGAYVA HPAVLTINAY IMINSYRWDW LMLLIIAISD LFVFFWTGVY TSFTSSSTFY
KAGAEIYGEA SFWACFFIVP VLCLFPRFSI KAMQKVFYPY DVDIIREQVF MGKFDYLKEP
KAKDDNKTDS RSQGSHGSSN RSSRRSRHVP YASVDEDLRP IYPPSTVTQN TYNGAHSQQG
SADTTNMPRY SVENPMHRIS TDRPRPSYDR MRASMDRTRA SFEASNDFTS AARLSRIESS
HSRGNSHSHT GIIRSRLRAL SSLSKKSDA
//
