ID A0A261Y4D8_9FUNG Unreviewed; 2097 AA.
AC A0A261Y4D8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=BZG36_01593 {ECO:0000313|EMBL:OZJ05334.1};
OS Bifiguratus adelaidae.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Endogonomycetes; Endogonales; Endogonales incertae sedis; Bifiguratus.
OX NCBI_TaxID=1938954 {ECO:0000313|EMBL:OZJ05334.1, ECO:0000313|Proteomes:UP000242875};
RN [1] {ECO:0000313|EMBL:OZJ05334.1, ECO:0000313|Proteomes:UP000242875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ0501 {ECO:0000313|EMBL:OZJ05334.1,
RC ECO:0000313|Proteomes:UP000242875};
RX PubMed=28876195; DOI=10.1080/00275514.2017.1364958;
RA Torres-Cruz T.J., Billingsley Tobias T.L., Almatruk M., Hesse C.,
RA Kuske C.R., Desiro A., Benucci G.M., Bonito G., Stajich J.E., Dunlap C.,
RA Arnold A.E., Porras-Alfaro A.;
RT "Bifiguratus adelaidae, gen. et sp. nov., a new member of Mucoromycotina in
RT endophytic and soil-dwelling habitats.";
RL Mycologia 109:363-378(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 -!- 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}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
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:OZJ05334.1}.
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DR EMBL; MVBO01000017; OZJ05334.1; -; Genomic_DNA.
DR Proteomes; UP000242875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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; 2.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000242875};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 859..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1518..1537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1549..1570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1600..1624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1636..1656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1663..1684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1704..1723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..387
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1486..1732
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1955..2081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1968..1985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2054..2081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2097 AA; 234005 MW; 0AB40246C8739F8B CRC64;
MTENHVDNGH EASTLSPSTP TPVARRKERT LQTHLQPLYS DLHSFSQDLD ETIWSMKALR
TLKEQVEGEL QGFSERYGRT SQSLANLQES QTNAQLVLEE QFFDLLHKAQ QVLDTDGQQD
PLEDNVDPSS LDAPSADPSL PSRPSTTAHD LKHLHLTMNK LLSTYSALAH RLDSIHSRQN
KSFRDISDIL TNVEQVQHLL LGAQSTMTEM ASPTSTGDTL SLWEDAQWPW QAEDDDEEEE
IHDDAMVLDE LEPRIMFLPY SRPTIRETPL KDTQEPSTEP NDDSPSRHNT AMERIKRLNR
RRASTPAVHK PSRRVFVNME LPEEATDEYG QPAQVFCSNK IRTAKYTLWT FIPKNLFEQF
RGIANLYFLA TVILQAFPIL GATNPGVAAL PLIAIIVITA AKAAFEDWKR AKSDEAVNKA
TTMTLAHWKN VNVLTGAVSN RQWIAHRIAS FMEQIGSIFR PSTRVGTQAM LGGGGKVDKE
AEDGDSVVDD PDFPNAVPHR DDTPEDVSDL SDSDNPRRFS TESRDDTGQR MPYRPGTIPH
SVVRRTATVE TTASQPYGQA SGAISDDNLS HPMSRLASIH TNADSGIPNP NSREYQECHH
EGSILQRIAT FRSGTSVYQE PAWTPTQWET VKVGDYVRLR NDESVPADVI ILASSEPDGL
CYVETKNLDG ETNLKVRRSL NATNELQSVQ DCIDAQFWVE SEPPNPSLYS YSGVLKWIVS
SGSNSHLKAP PSTTRRQSVK PSISQPVTTP QSELNRNLDH IPEHPNDSLE AAPRHSMQSN
RGNPLASSTS IPRLHHGVTH EKTEAITNDA VLLRGCVLRN TDWVIGLVVY TGEDTKIMLN
SGRTPSKRSK MEKGTNPHVV ANFGLLAILC IVSAVMNSIY YRNVTTADFF EYGQDANSSG
LSGFLTFWVT LILYQNIVPI SLYISVEIVK TLSAYFIFSD VDMYYAPTDQ PCIPKTWNIS
DDLGQIEYIF SDKTGTLTQN VMQFKRCTIN GVAYGLGETE AMEGQKKRLG LDMEKQDTKR
LSRTMTGSTQ HHVSDMNGSS RQANDAPSSE ESEVTKHDEE TAVEDEEDGS GLGRAKQQMK
EMQSELFENK YASPMPDFVD PKIFQDLAAD DAQSRAIVQF CSALAICHTV LPEFPDPDNE
FKVEYKAQSP DEAALVATAR DLGFAFLGRE QDKVTLEAMG ERKQFVLLNV LEFNSNRKRM
SVILRSTEGE GRLVLLTKGA DSVIYERLAN EFGDNEDLKK AQSKIREATL KHLEEFANQG
LRTLCLAYRF VSEGEYHQWN HRYQDAAASI SDRDEKIEAV CEEIEKNLLL MGGTAIEDRL
QEGVPEAIAL LSKAGIKIWV LTGDKTETAI NIGFACNLLE QDMTLIIING DSKESAAQQI
EDSLVKFWEE DTDGWAKRHA LVIDGETLKY SLEKDVRPRL LELAKRCKSV VCCRVSPMQK
AQVVNMVRKG LKVMTLAIGD GANDVSMIQE ANVGVGISGE EGRQAVMASD YAIGQFRFLS
KLLLVHGRWS YLRTAEMIFA FFYKNIVWTL VLFWYQLFCG FTGTMMFDYS YITLYNLVFT
SLPCIVLGVF DQDVGTQLSM QNPELYYMGL RNVKFTVLRF WLHILDAIYQ SAVCFFIPYG
VFVVSNISED GLFTNGVYEL GTFIAGIAVV VANGYVSITI FCWTWLMAVI IFGSMATYFL
WVAIYSPFNT FTFAGQSTLF GDVTFWLTLI ITFAICMGPR YAVKHIIHQY WPFDNDIIRE
AVLCKQGKEH EEEDMMPINP PPYQQAESGV TSGRPTLSLI RTQSMDDVEF MNYANPNVTN
SVPSPAPAFR RAAHRRTPSA GSTRSDQLNY MSSGKRMSFT GFAYSADEDS AFHTYRRSVY
HPGAASSQPD VSSAYAAAMA TERFLNRTRS TSKSSDYTKK MGEDWMMLQP VKISRTESAP
VPFTQDRRKR FSPTHAIGHA MSSFASSISG LPSHTFNPHN SFHRSGSNLR HAVEETEEER
QEVQPDSNHL TVPGTSSSQP PSKRHLSGSL GKMSRRLSNS FRQTVSPSVK ASPPTPAAAP
AIHPHPPSQQ PLTVPSPAAQ SNVSQGSDRP STPGSSYFPD LISHDTIYSS LNHNPTP
//
