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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