ID A0A4U0TUW9_9PEZI Unreviewed; 2005 AA.
AC A0A4U0TUW9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=B0A54_17347 {ECO:0000313|EMBL:TKA25772.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA25772.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA25772.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA25772.1,
RC ECO:0000313|Proteomes:UP000310066};
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 -!- 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 RNase PH family.
CC {ECO:0000256|ARBA:ARBA00006678}.
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:TKA25772.1}.
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DR EMBL; NAJP01000151; TKA25772.1; -; Genomic_DNA.
DR STRING; 329885.A0A4U0TUW9; -.
DR Proteomes; UP000310066; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:UniProt.
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; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 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; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR036345; ExoRNase_PH_dom2_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 InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
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 Pfam; PF01138; RNase_PH; 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 SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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:UP000310066};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
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 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1164..1185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1215..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1256..1274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1281..1301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1321..1341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..147
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1101..1350
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT DOMAIN 1720..1885
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2005 AA; 222978 MW; C2D8A21AAE21CC52 CRC64;
MAISPYAEDS ERTNPVKRIR WATQRVTGRK GVEKRKSIFR RHNARNSTIE KNRESSGTDP
GLVKPTQEDP PAGEKVEAAA QPGRVIYFNI PLPDHQKDDE GRPIQHFKRN KVRTAKYTPL
SFVPKNLWFQ FHNIANIFFL AIIILNVSWL RNLRTLSKPD LSRDTVLLLD NELNNASVHR
LTDWDNVNTA DEYINPWRRL KKATTRGLMW IWRSRRNRKE KKQAKKEGIA RGLTESGLDD
SPESEYDDRR FSELTQRLDK EESHPGEDAN GDVEMAPVPS PIPSQHRSGD KGYMDGVDVE
QLPNDAAGRG DAHQTLEVIR DNRHPDVPVI TKKFYGSLID PTRETQEKGR FKRDMWKNVQ
VGDFVRLYNE EQIPADIIVL STSDADGACY VETKNLDGET NLKVRTALHS GGKVKRARDC
ERTAFTLESE PPHANLYTYS GVVRWNQRNP AHPDEPAKAM AEPVGINNML LRGCNLRNTE
WVVGIVAFTG EETKIMLNSG ITPSKRARIS RDLNWNVVYN FIILFVMCVV AAVVEGSTWA
HGHESLDFFE FGSYGGSPPL DGLITFWAAI ILFQNLVPIS LYISLEIVRT AQAYFIYSDT
YMYYEKIDYP CTPKSWNISD DLGQIEYIFS DKTGTLTQNV MEFKKCTING TPYGEAYTEA
LAGMQKRQGI DVEAEGRRAR EQIATDRVTM IERVRRMHDN PYLQDDELTF VAPDFVADLG
GEGGPAQRAA CERFMLALAL CHTVITERTP GDPPKIEFKA QSPDEAALVA TARDVGFTVM
GRSNEGIIIN CLGEEREYTV LNTLEFNSTR KRMSAIMRMP DGKIVLFCKG ADSVIYSRLK
KGEQPELRRQ TAEHLEMFAR EGLRTLCIAQ RELGEEEYQK WNIDHDLAAA AVQEREEKLD
AVADTIEREL TLIGGTAIED RLQDGVPDAI QLLAQAGIKL WVLTGDKVET AINIGFSCNL
LNNDMELIVL KVDDENVQAA EGTLDQELAK FGKSGSDEEL KAAKKNHEPP APTHALVIDG
DTLKLVLDNR LRQKFLLLCK ECKSVLCCRV SPSQKAAVVQ MVKAGLEVMT LSIGDGANDV
AMIQEADVGV GIAGEEGRQA VMSSDYAIGQ FRFLTRLMLV HGRWSYRRLS ETIANFFYKN
IVWTFALFWY QIYTNMDCSY AFDYSYILLY NLAFTSLAPI FMGILDQDVN DKVSLAVPGL
YRRGIERAEW TQLKFWTYMA DGLYQSLICY FFTYLIFRPA NFNTESGHVI SDYKRMGVFI
GNPVVVVVNI YILLNTYRWD WFMCLITGIS ILLIFLWTGA YTSFTDGFTF YGAAKQVYGS
LSFWAYLLLT VVLCLLPRFS AKAFQKIYYP RDVDIIREEI RQGKFDYLKD IDPADLDPLA
AAKKAESTSS SSEGSNSAAK KAKTSQQQQQ QQHQHALSDD MRPMYPPSVA VTATTRGGGG
GQGGADNTHS QNGSDGTDYT GHRSSLDRAF PPSASHQYSH SVPFAAGTTL HPLAPAITAE
DLEGPPQRNL ARNSLDRPRP SFDRLRSSMD RTRASIENSR DFTSAAYLAR MESSESRGGG
GGGGLSAPGE GVAGGVGAGA SRRRDVIPLE MIFISVSLGE YLPRDCTSSQ ALQTLYDPKI
WVTNQSGMDL SEAALGNLRF TVATVWVKSK RRQAAAAFPQ KLVDGRQTVH TKGGKYNAHA
PTGLAFSRET FAKLTPGPFL QAHLQQPEPI RPNGRSLHAF RTPTIHTGSL SHSNGSAVVR
LGDTAVVCGV RAEILLAADI PHPPSEDTSE DDLVERLGLL VPNVELSTGC SPDHLPGNPP
STSAQALSYR VLSLMHTSNL IRPGDLSIQY MEPASDDDLP DEGPKTVTKA FWTLYIDVLC
IALDGNPFDA AWAAVISALK STRLPRAWWD PDREMVLCSP LANETHGLRL DDIPVASTFA
VFSTGSALKQ RSEAESWVLA DPDGFEEGVC TETATVVVRS EDGDAGGITR LEKSGGGAIG
KAAMGRCVHM AQQRWREWQG VLHGG
//
