ID A0A2B7WMS2_9EURO Unreviewed; 1300 AA.
AC A0A2B7WMS2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=GX51_05650 {ECO:0000313|EMBL:PGH00664.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH00664.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH00664.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH00664.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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: 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:PGH00664.1}.
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DR EMBL; PDNC01000082; PGH00664.1; -; Genomic_DNA.
DR STRING; 2060905.A0A2B7WMS2; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000224080; 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; 1.
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; 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; 2.
DR PANTHER; PTHR24092:SF5; 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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000224080};
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 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1098..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1124..1146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1176..1194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1206..1225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1232..1252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1264..1287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 182..233
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1064..1292
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 144092 MW; 9FE4E4FB7FAE6CF9 CRC64;
MARTHEYKQP SAQDVSDDAE SDEDLDLNEL DPEAAGSLYN GHSPTSREIR TAPAYGSGIA
LRNLRAGARD RIWNRSADRT RRQDGEEDND YLLDDRDGAN QELSGRSSTY ADDDMPLLNG
RSQPRPNPTP NRSLYSRLRS RLRFLRFGSS PQLDTTPDGY DDLPLHHNPN HGPTRKVLVG
QTQQTRYPPN VVSNAKYTPW SFLPRTLYNE FSFFFNIYFL LVALSQIIPI LRIGYMSSYI
APLAFVVSIS LGKEALDDIA RRRRDAEANA EEYTVISFTP SSSRKPVVRN TVAVSDQGSV
LHGNKIFEIT KKSRDLKVGD ILKLGKDQRL PADVVILKSA LPEVAAAQNT NHTGQLVDRD
NDAAESTEDC HITPQADESA DDIDGSSDTF IRTDQLDGET DWKLRLPSPL TQNLHLSDLQ
RIRIIAGEPE KSVHSFVGTI ELTPPPNSYD PHINKTDATS RSPTRSLSPD GHHQNLPELQ
SAPLTIDNTA WASTVLASNT TTIAAIIYTG AQTRSAMSTS PSRSKVGLLE YEINSLTKIL
CILTLSLSII LVALQGFEPS NDKPWYIAIM IYLILFSTII PMSLRVNLDM AKSVYGRFIE
RDTGIPGTVV RTSTIPEDLG RIEYLLSDKT GTLTQNEMEL KKIHVGTVSY ANEAMDEVAS
YLRQGFSTAP SSHEPRSSLV TPTTINGAQT GLASTTRTRR EIGSRVRDII LALALCHNVT
PTTDEQNGEK VTAYQASSPD EIAIVKYTQE VGLQLVHRDR QNIVLKSITT GNVVVRVRIL
DIFPFTSESK RMGIIVQFKQ GSDLDKSAAQ DEEIWFYQKG ADTVMSSIVA TNDWLDEETA
NMAREGLRTL VIGRKRLSQA QYQDFSTSYK QASLSLHNRD TGMAKVCQEY LEQNLELLGV
TGVEDKLQKD VKPSLELLRN AGVKIWMLTG DKVETARCVA VSAKLVARGQ YIHTVTKLKE
KGSAQDTLDF LRNKPDSCLL IDGESLTLML AKFRTPFISV AVLLPAVIAC RCSPTQKAEI
ATLISQHTKK RICCIGDGGN DVSMIQAADV GIGIVGKEGR QASLAADFSI TQFHHLTKLL
VWHGRNSYKR SAKLAQFIMH RGLIISACQT MYSIAGHFDP KGLFINWLLV GYATVYTNAP
VFSLVLDRDV DEELANLYPE LYKELKTGRS LSYRSFFTWV LVSVYQGSII QGLSQILVGD
VTGPKLISVS FTALVLNELV MVAISITTWH PVMILCILGT AVVYAASVPF LGDYFDLEYV
VTLAWLWRVI VAAAVALIPV WAVKFISRTW SPPSYRKVRG
//
