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Database: UniProt
Entry: A0A1Y2WH38_9PEZI
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Original site: A0A1Y2WH38_9PEZI 
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
//
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