ID A0A167M369_CORFA Unreviewed; 1542 AA.
AC A0A167M369;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=ISF_08561 {ECO:0000313|EMBL:OAA53859.1};
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:OAA53859.1, ECO:0000313|Proteomes:UP000076744};
RN [1] {ECO:0000313|EMBL:OAA53859.1, ECO:0000313|Proteomes:UP000076744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2679 {ECO:0000313|EMBL:OAA53859.1,
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:OAA53859.1}.
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DR EMBL; AZHB01000032; OAA53859.1; -; Genomic_DNA.
DR RefSeq; XP_018700628.1; XM_018852164.1.
DR STRING; 1081104.A0A167M369; -.
DR GeneID; 30024853; -.
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 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; PF00702; Hydrolase; 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 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 474..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1235..1258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1288..1310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1322..1343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1350..1369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 177..235
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1174..1425
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1542 AA; 173206 MW; 99C11A09824E570D CRC64;
MLPNRNSASA GSGHHVPAVA AVDATVDTQR SATPRMTASR SNTDPTVALS RGTGAAARAH
VGQHELETIH SKAPLAAATK TDSVDDAATS AAASTSVRLA KPSLRDRLGH LRPELLASNK
RRRQMHGMLW KEKAKARVAA AYQSVIIEGL LRRKPLPPSR DGRHIPMNHP DSLVDERSSR
HYCSNFIRSS RYTVYDFVPK QLLFQFSKLG NFYFLVMGIL QTIPGLSTVG QWTTIGPLLA
FVAFSMAKEG LDDYRRYQLD KSENRSNTLV LSRNDGRKRK PAHMKTAMKR IKYFNDKDEV
AVEEIALGDV EQSPANSDWV ELDWQQVRVG DIVRLQRDED VPADMVLLHA TGPNSVAYIE
TMALDGETNL KAKQACPPLA ERCATVDGLR KTQATIVSED PNIDLYSYDG RVVIGSETLP
LTLNNVVYRG STLRNTSEAI GLVVNSGEEC KIRMNAHKNV RTKKPAMQSA VNKIIFFQIF
IVVMLAVGFT IGYYLWEEDV ENKSFYLYRK GVYDAAVPFR EIFFGFLIMF NTLIPLSLYI
SLEIVKLGQL LLLHDADMYD PVSDTPMVAN TTTILENLGQ ISYVFSDKTG TLTENLMRFR
KLSVAGVSVL HDMDVLRDER AKQDKLNTYK TSKKRGRQQA NAVTSAEPVG RTSTGSLTHW
KSSVRPNDEP DMKTEELLEY IHLKPNTAFS RKAKHFLLCI ALCHTCLPES KDDGSIHFQA
ASPDELALVE AAQDLEYLVI DRPAQTIKLQ IKDAEGNKAV ESYQVLDVIE FSSLRKRMSI
IVRMPDKTIC VICKGADNVI TSRLKLSHLA EQKARDIGHR ASMRKTFEKN KALQRMSMQM
SARSTPRNSL TIRNRDSTDF REGLRQSIGR RSVDGNRLGE GQSSWLQRRR TEEMATPRHS
VDLLKSNRRS LSRVASFDAI DRRVDESIAS SDAAIFERCF QHVDDFATEG LRTLLYGYRY
IDEDTYAKWK AQYREAETSL VDRQQRIEVA GDLIEHKFDL AGATAIEDKL QDGVPETIDK
LTRANIKVWM LTGDKRETAI NIAHSAHVCK PYSELYILDA NAAGALTDQL TMTLTDVSRG
MAPHTVLVVD GQTLTKIDAD DELSILFYDL VIRVDSIICC RASPSQKAEL VKAIRRYVPG
SMTLAIGDGA NDIGMIQASH VGIGISGREG LQAARISDYS IAQFRFLQKL LFVHGRWNYL
RTGKYVLATF WKEIFFYLLQ AHFQRFTGYT GTSLFQSTSI AMFNTLFTSL AVILPGIFER
DLRAETLLAV PELYTFGQRN KAFNYRLYIG WMLMGIASSF IVYYITWAVY NSALFTEDTS
LYAMGTICFT VGVIFINTKL FILELHSKTV ITFAGYIITI GGWFIWLLIL NKLMSASMNV
YLVHDAFTRN FGTHLGWWTT LLVALTGPIM LELVVQGVRR VYWPTDTDLM QRMEKDADVL
EIQARFDRDP EAHHTHASDD EQVIPDDHRG GRAGLGAAKV SQELERGAAV PGRFSLSDTP
RRPPAVRASL DEYRPSQFTP LTEEQENPST KPSTKLERIR DD
//
