ID A0A1Y2WH38_9PEZI Unreviewed; 1396 AA.
AC A0A1Y2WH38;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=M426DRAFT_317370 {ECO:0000313|EMBL:OTB08256.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB08256.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB08256.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB08256.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ111527; OTB08256.1; -; Genomic_DNA.
DR STRING; 1001833.A0A1Y2WH38; -.
DR InParanoid; A0A1Y2WH38; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000242955; 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 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 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:UP000242955};
KW Translocase {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 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1226..1244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1256..1282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1302..1321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 85..142
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1080..1328
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 551..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 156799 MW; D8DB438264CF0824 CRC64;
MPRMADHEDL DVAKKQDTDT ISTAARKTRK RFEELGGVVE ECATQLYKKY VIELLLRQKP
LKPSKDGRHI PFRVEQDEVL IDERRGHPYI PNTIRTSRYT LIDFIPKQLI FQFTRLANFY
FLCVGIPQAI PGLSTTGSYT TILPLLFFVA LTIVKEGYDD YKRHRLDNLE NANAATVLRR
KSADINPVLS TRKWFPGRRK TVETTVQPLE DEVDSEFGWR QVKWQDVKVG DVVKLVRDDA
VPADLVLLHA SGEDGLAYID TMDLDGETNL KTRESLAEFS CCDTIAGLRS CQAEFVLEDP
NPDLYRFDGR VAVNSQTLPL TSNEVIYRGS TLRNTARAIG VVINTGEECK IRMNANQHPR
AKKPALETIA NKIVITLALY VIILTVGCSM GYIIWRPTER ISWYISMATV EFKQIIIGYA
IMFNNVIPLA LYVTLEITRI GQMLLLNGDV EMYDEATDTP ARCNTNTILE NLGQVSYIFS
DKTGTLTENV MKFRKMSIAG TSWLHEADIN LETPVVMTPG LNADAAVAMP RRSREVSSVI
HEDVELYPLS PSSSAFSPQS ERRSSSQWRS SGRPDLPQPD VTTADLLEYI KLRPASSFAR
QAKDYILCMA LCHTCLPEVE DGKVDFQASS PDELALVRAA QELGYLVAHR TSQSVTLQID
IGDGNKRTEV YEILDVIEFS SKRKRMSIIV RYPDGRICII CKGADSMVLP RLKLAQLAAQ
KATEVRKSVE AERELIRRSE QLDVRNSFGG RPSLTLRRNM AGNRNSITIA QPTIVVQKPA
MVRSRSAEGS RTRLSEQKSR PSLGIRTTSL DVTKTLLSPS TPRPAPDKFS FLDDPSILDD
STTFSRCFKH LDDFATEGLR TLLFARKFIS ESDYEAWKKI YNNATTSLVN RQDMIEAAGE
LIEQSFDLVG ATAIEDKLQT GVPETIDKLR RANIKIWMLT GDKRETAINI AHSARICRPG
SDLFILDSSK GSIETQITDV TEDIAAGCTH SVVVIDGQTL QIIEQSPHLT NLFYTLIPSI
DSVICCRASP AQKSVIVKAI RQRVPSALTL AIGDGANDLA MISAAHVGVG ISGKEGLQAA
RVADYAIAQF RFLQRLLLVH GRWNYVRTAK FILTTFWKEM YFYLPTAMYQ RYNGYTGTSL
YENWSLTVFN TLFTSLCVIC LGIFEQDLSA ETLLAVPELY VHGQRNRELN IPRFVRWMAA
AAAQGVLVWL GAWAAYSVYG TARDNALFAF GDLVFTVGVL WINCKIFLLE THNKTSVVLG
AFGITMAGWW VWNAFLSGAY PAQTSPYPAR DGFTTTFGKD PLWWLTIIVE VLVLVSIDLV
YKAIKRNMII AGTWKWPPWK RRSVDDSLEE WGLDVWQEVE KDPVMRERLR RACVEDLDIG
DERLDSVEAD DVAKVL
//