ID F2TDT8_AJEDA Unreviewed; 1750 AA.
AC F2TDT8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=BDDG_04343 {ECO:0000313|EMBL:EGE81401.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE81401.1};
RN [1] {ECO:0000313|EMBL:EGE81401.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE81401.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) 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}.
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DR EMBL; GG749426; EGE81401.1; -; Genomic_DNA.
DR HOGENOM; CLU_000846_5_3_1; -.
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; 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; 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 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 624..650
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 670..691
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1469..1496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1502..1519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1531..1550
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1575..1595
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 329..386
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1355..1605
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1750 AA; 195103 MW; E42C6865E34B2B4B CRC64;
MAGRDGNNPG LGRLDSPRLP RRASSRSPLR DSILREGGAD REEDGTVLLQ DAGGGRTTGD
AGDIGASTHT DTTDRASSQD TRRPSQARVR FSVDLERTPD NTIPPSPRCE ESQDSAGRDV
GGGSGRAAGL GLRVDTSLPS VISKQRSPSL RSSGQWISPV SPVSPTDPLP PLHESPPLVL
PATRNRGYSL RRAIFNRNIA NQSEHDQTDN IELRHQLSAG GEPLSRVHSQ PQIQHGAGQE
VVFPTSSKDE ESTTFSDLKA QLRERKPYSA GRAAACKVRA THELAVGKLK VVTDAFRKHV
LRIKEIPPSK DGRHIDLDVQ RQEPRIDERT GKYYVSNHIR SSRYSLWSFF PRQLVAQFSK
LANFYFLVVS ILQMIPGLST TGTFTTFVPL MIFVGISMGK EGIDDLRRYR LDKEENNRIA
YILRARNANS NATAATTATT SKTTSTTSTD AMEAKITSTT DTDSYSNSAG YWAPTKWVDI
KVGDVIKLSR DQPAPADIVL LHADDPNGIA YIETMALDGE TNLKSKQPCR PVAKTCKTAE
DIIHNTSIHF AVEDPNIDLY KFDGNVTVGQ EKLPITNSEV IYRGSILRNT HEAFGMVIYT
GEECKIRMNA NKNPRIKAPA LQTVVNRVVA VIVLFVVVLA SACTIAYTFW SRDVEDKSWY
LEEADVSIGP IFTSFIIMFN TMIPISLYVS LEIVKVAQIF LLNDIDMYDV ESDTPLEART
STINEELGQV SYIFSDKTGT LTNNSMKFRK MSVAGTAWLH DTDLQEEAAR DADRKMLLHK
KRKEKKASSR KSSTYDQVTF GRKSGVSNHR QEENSSPTAT TTTHWRSNRR GRMYHGGRTV
EMLEYIQQKP HTLFARKAKF FILALALCHT CIPERDDDGD ISFQAASPDE AALVTAAKEM
GYLVVDRQPN SLTIRLSTTA QDEDGEPVAE EEVYEILDII EFSSVRKRMS IVVRMPDQRI
CLFCKGADST VMGLLKRSGL AAEKVAEIEN RANKRKSLEA KEVMRRNSEH AHRKDGKTSM
SIGRPSFAAG RRSSVSGKRR SSLRDSIDVW LRDRETDGGL VLRDGDDDYY YSPRPSMQLS
PRPSGALSEE RYRASFQTDD GAEDLVEESL VVNEAMVFER CFQHLNDFAT EGLRTLLYGY
RFIEEADYQE WKARYHEATT SLVGRQEKIE QVGEQIETQL ELGGATAIED KLQKGVPEAI
DKLRRANIKL WMLTGDKRET AINIGNSCRL VKDYSTVTIL DHDAGDVERV ILETTSEIVR
GACAHSVIVV DGQTLSTVEA DAPLQELFFD LAILADSVIC CRASPKQKAF LVRSIRKRVK
RSITLAIGDG ANDIAMIQEA HVGIGITGKE GLQAARISDY SIAQFRFLLK LLLVHGRWNY
IRVCKYTLGT FWKETVFYLT QALYQRWNGY TGTSLYESWS LSMFNTLFTS LPVIFLGIFE
KDLAASTLLA VPELYTKGQR NGGFNVKLYL GWAFMGSCEA MVVYFTMYGL FGSAIFTLDN
RVFAMGLLTY TACVIIINLK LQFLEIRYRT VMAAIVIIVS IGGWFLWNII LSRRYALDAI
YNVRDNFLPR TGRNLLWWVT LLLAVVAVLL FEICVTTLRV ALFPTDVDHF QEFEGDLEIR
KRFEEAAASE LQQGWDRGKK SGLETMTDLN GGDVADMEAE REREMQVQEL LDRRSAPRGR
GKGKGGDGAD VQMEEVELGN GQAFVNGGGG GAGRAAEESG DVSSPSPSRR SLDIQELLNR
RFGAIWKGQL
//