ID A0A1Y2B225_9FUNG Unreviewed; 1428 AA.
AC A0A1Y2B225;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=LY90DRAFT_513101 {ECO:0000313|EMBL:ORY28547.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY28547.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY28547.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY28547.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ORY28547.1}.
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DR EMBL; MCOG01000185; ORY28547.1; -; Genomic_DNA.
DR STRING; 1754190.A0A1Y2B225; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000193920; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
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; 2.
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:UP000193920};
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 431..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1228..1246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1294..1315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1327..1346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1366..1399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 163..226
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1107..1255
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT DOMAIN 1285..1395
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 83..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1428 AA; 163680 MW; 33C89DE04D174293 CRC64;
MSNFGYSNNQ YTTGSFNYLQ PNSVEDDNNS IVYPESTISV KPLIDNNTNK QLENNYTLNN
KTQPDYIELN EVNTTRIVTN KMSSSNQQYH SPTNTSFSEL PKSPTRQSVT LENRTNKRRP
MSIASRTSRL SRVSTLSRIY QNEQVGRAIY VNSTKQSKNF DNKKKRTKRK GEFITNIVRT
ARYTIANFLP KQLVAQFSKL ANVYFLFISV LQVIPDLSPT GRFTTLAPLC LFVALAMLRE
AYDDYHRHKQ DNMENNCIAK KFFKYANGKY EWRNIPWKEI SVGDVIYIGN NEQIPADVVV
LASSNDKGIC FIETASLDGE TNLKQRQALK ETTDLIYDEE TLNDFSCKIQ SESPHEDLYN
FDGYVEIYDS SEQERVPLTI SQLLLRGATL RNTNFIFAVV IFTGEETRIR LNASKGIRTK
SPALDKFTNK IVVSLFIAVL GIGLITLLMS LYWNKTHKPG PNAHWYLKPE GSKPSAFRQY
LTDTVLFNTL IPISLYVTLE ITKLVQVYFM NNDLEMYDEE SDTPCEARTS SLNEDLGQVR
YVFSDKTGTL TENRMVFKNM SIGGVSYLHE FNNTKNMDIA SSKAKNSSNE SLSKYNNNQF
NRSESPLTLS TSNNDLENYD TGNITSSIQE NSVRTEKLIN DLMINNGNWT DKQNEVIDFL
IGMALCHSVV PENQDKKKEN AENECLRTSL ARIDYNPNDI NDDNNQSEDF NYNDNFHITY
QSSSPDEMAL VTAARQMKVI LTDKSMTDIS LNILGQHVDT QYRLLNTIEF SSARKRMSTI
YEYPDGRIMI LCKGADSVIL ERLKNREDMT EDERRVLDIT NDHLTQYSIE GLRTLLYGIR
EISLKEYEEW LNIWNEASTA LTERSEKIAK AAEVIETDFS LLGATAIEDK LQKDVPKTIE
KLREAGIHVW MLTGDKKETA FNIGMTCRII KENSIIFRVE GRNITEISQV MDKALEDIEN
IKINNKKRRN SDHTVVIIDG DSLLKIERDA ETQARLSDNN AKESDSKKKK IEIHRKLPTG
NLLKFLDLSC RADSVICCRF SPSQKALIVA SIRNILMKNP TFASSGEYSK NSSAVTLAIG
DGANDVPMIQ AAHVGVGITG REGLAAARAS DYSFAQFRFL QPLLLIHGHY DYIRVCRFLL
GTFYKCTAFY ITQFLFQIFC GWSGTSLYEQ WTLSLYNVLF SSIPVLIVGA LEKDVEKETL
LANPKLYQYG QHNLALTWKT FWRWLIQGLW HSICCVFIPF ILYNGFTPLR TTKYYDNVVD
ANGMITYFKK EGLAWNIKKL FNSDGAMNLQ DNSLFFLGTV VFTSAVFVVT IKICYIENHN
HTIFTHLAAF LSLFFWFGWN FIYYRFGHII NFGENVHYLW YNVFSSPAMI IQASLTVLIT
VVTAILICDY SFAVIWSWFD LDKNRGSESL DIELCQRWEK NIRKRRHY
//
