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Entry: F2TDT8_AJEDA
LinkDB: F2TDT8_AJEDA
Original site: F2TDT8_AJEDA 
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
//
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