ID A0A1V8SLW3_9PEZI Unreviewed; 1281 AA.
AC A0A1V8SLW3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B0A48_14221 {ECO:0000313|EMBL:OQO00018.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO00018.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:OQO00018.1}.
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DR EMBL; NAJO01000037; OQO00018.1; -; Genomic_DNA.
DR STRING; 1507870.A0A1V8SLW3; -.
DR InParanoid; A0A1V8SLW3; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000192596; 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; 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; 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; 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:UP000192596};
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 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1100..1117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1147..1169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1189..1207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1214..1240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1246..1263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 158..207
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1035..1273
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 139829 MW; 6492C69D187E5157 CRC64;
MNRQQQRSEQ GYNDPDSDLD LDLEELDPVS SSHSPPRRQA RSSTDYSGRI PLRNLRHGGR
RRQRVVEDDL EPLVADEDAL GKREEHAGDD APLLANGSLR RGSLLDLDAE ARSRGWKARL
RRLLPFSKRH NAIALADETS EDSTATNRTI QVGSRQLTPF PANAISNAKY TPISFLPVTL
WNEFKLFLNL YFLLVALSQV LPALRIGYLS TYVAPLAFVL AVTLGKEGWD DVMRRRRDGE
ANKEPYVVLR LEGHGRAGTA KGKSLSGSKG VKRRKGDRTA ELEREEEAVG LEDEPSARVI
EVRKSAKDLA VGDVLVLEKN QRVPADVIIL KSIATDAAVS EDVSSAPSRT SEALMDLGEE
AGDELHTPMP PNEPAPDAGG EAFIRTDQLD GETDWKLRVA ASLTQSLSAS EYLRLRITAG
KPGKRVNDFA GTIELLPKSS AAYDPQPSEI TDAPTTTTAS APLTIDNTAW ANTVLASSTK
VYAVVLYTGP QTRAALSTAS SRSKIGLLEL EINSLVKILC ILTAALSLLL VALQRFENDD
EERPWYVSVM RFLILFSTIV PISLRVNLDM AKSVYAYLIH RDQGIPGTVV RTSTIPEDLG
RIEYLLTDKT GTLTKNEMEL RKVHVGSGSY GGEAMDEVRE FVRLAFAKEE GAADGALWTP
SSGYGGLANA TRTRREIGVK VRDLVLALAI CHNVTPTIDE TADGEKKTSY QASSPDEIAI
VQWTEAVGLR LAHRDRRTMT LHFAGAPVVK VEILNIFPFT SDSKRMGIIV RFYANLSHQG
DDVVFYQKGA DTVMSPLLAP NDYIDEEVGN MAREGLRTLV IGRKALSPTA YEAFTRAFHA
ASLSLTARDK AISRVLSTHL ESSLHALGLT AIEDLLQPLI KPSLETLRNA GLKIWMLTGD
KPETARSIAL SARLVSARSQ TIHPILALRS PSLCLPALQP LLASPSTTAL LIDGASLVLY
LTHRPSAFLS ATLPLPAVIA TRCTPSQKAS ITTLIRSATG KRVMAIGDGG NDVSMISAAD
IGIGIEGKEG RQASLAADFS VTQFSHIVKL LLWHGRNSYK RSAALGQFIM HRGLLISVAQ
TVFSIHLAGE PVALYRDWLL VGYATVYTMM PVFSLVLDRD VDERLTNLYP ELYHELQAGT
SLSYRTFAVW TGISLYQGLV IQLGAQLLAP SPTPGSSPSS TLPDSRMLLL SYTALIINEL
LVVAASIETW HWSMWVSILS TALLYAASVP FLGGYFSLAW VIEMGFWWRL AVLVGGSVGP
VYVGGRVRRW LRPGIVGKVR G
//
