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Database: UniProt
Entry: A0A166NWI2_9HYPO
LinkDB: A0A166NWI2_9HYPO
Original site: A0A166NWI2_9HYPO 
ID   A0A166NWI2_9HYPO        Unreviewed;      1621 AA.
AC   A0A166NWI2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=AAL_05932 {ECO:0000313|EMBL:KZZ92900.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ92900.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:KZZ92900.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ92900.1,
RC   ECO:0000313|Proteomes:UP000078544};
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:KZZ92900.1}.
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DR   EMBL; AZGY01000014; KZZ92900.1; -; Genomic_DNA.
DR   STRING; 1081109.A0A166NWI2; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000078544; 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; 2.
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; PF00702; Hydrolase; 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:UP000078544};
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        514..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        562..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1350..1372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1384..1406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1413..1438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1458..1478
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          224..281
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1236..1488
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1535..1570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..681
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..970
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1548..1570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1621 AA;  180983 MW;  4C8AD81A75EAE593 CRC64;
     MAPMEPNNRN HGSSIIPPPS SDPRNEAIDL APSQADVQAQ DSQGHSWGQI ASIRRSSADA
     TAGLPRAATF PRSSRRRSLA ADSNAALGHE QHVLSPILSR VPMADIAPGP AASGGRHGAE
     GEQGGGTPEK VHVVASAASI PNYAGSNTGK SFRQSRSSRS REKEGFVRKH RKSAGWTEGA
     KIRVAAAYER LIIKGLLGHR TLSPSLHGRT IPLNPPAILV DERSQKPHIS NFIRSSRYNV
     YNFVPKQLLF QFSKLGNFYF LVMGTLQMIP GLSTVGRWTT IVPLSIFVAF SMAKEGYDDF
     RRYQLDKAEN RSLTWVLRRG RDEGSNSGNS GGKRVWDFKK DIDLEGGVYA TMENGDSEWT
     LKQWQDVKVG DVIRLKRNDA VPADMVLLHA TGPNGVAYIE TMALDGETNL KSKQACSLLA
     EQCSTVEGIK SSPAVIVSED PNIDLYSYDG KVTVGGETLP LSLNNIAYRG SIVRNTAEVF
     GLVVNSGEEC KIRMNANKNV TAKKPAMHAI INKMVLFQIV IVLMLAAGFT IGYHIWKREV
     QSRSFYLVSS VRWSASVPFR DIFFGYLLMF NTLIPLSLYI SMEIIKIGQL ILLQDVAMYD
     PVSNTPMVAN TTTILENLGQ VSYVFSDKTG TLTENVMRFR KMSVAGVACL HDMDVQRDEK
     VKQRKIEASM LSRRKPDSRA ETHNSSFLMK STEHDTYTDD GYDDEESAPT KRKGSFASAS
     HWKSSVRPHE QPELKTEDML DYIRRKPNTV FSRRAKHFLL CIALCHTCLP EQQEDGELAF
     QAASPDELAL VEAARDMGWL LIDRPGQIIK LRSTDENGFL QIEEYQVLDV IEFSSKRKRM
     SIIIRMPDGR ICVFCKGADN VIVSRLRMSH LAEQKFKDIG RRASVRKTFE QDKARNRMSL
     ASVRDTPRNS TAIKRGDSID ALEGLRRSIG RRSTDLNRLS LHEGFSTRMT RQQPDEQATP
     RGSFEPHNQP RNSFGRRPAL DTIDQRIDES VAANDAAVFE QCFQHVDDFA SEGLRTLLYA
     YRYVDEDMYA DWKQLYREAE TSLMNRQERV EEAGEMIEQK LELAGATAIE DKLQEGVPET
     IDKLRRANVK VWMLTGDKRE TAINIGHSAR VCKPYSEVYV IDRHNGDLRD TLQTTLNDVG
     RGLVPHSVLV VDGQTLATID ADTSLASLFY DLALRVDSVI CCRASPSQKA DLVTSVRRSL
     PSSMTLAIGD GANDIGMIQS SHVGIGISGR EGLQAARISD YSIAQFRFLQ QLLFVHGRWN
     YLRTGKYVLA TFWKEIIFFL AQAHFQRFNG YSGTSLFEST SLTVFNSLFT SLPVVMLGIF
     EKDLSAETLL AVPELYTFGQ QNRGFNLLQY VGWMLMGVTG SFVIYYFTWA NYAMAISSLQ
     DTNLYAMGTL CFTVGVSFIN VKLLILELHH KTAITFGGFI VSVAGWFFWC LLLSGVFPQK
     VGKEMVRRSF IHHFGRELNW WTTLLIALAT LVILDLVVQS VRRVYWPTDQ DLMQRIEKDA
     GAREALREHA VRTEAGFLSD MEDIEMRDLN LVPGRVDGRR RSRTDKAESP SGSSSSSSSS
     SGNGHFTTVT YHGGAEERSQ KQTAHVSVAE CAQTPAIPAA FDKKEGVFGR LKTKMKRVGK
     L
//
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