ID A0A0V1KUD2_9BILA Unreviewed; 1261 AA.
AC A0A0V1KUD2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=T02_7536 {ECO:0000313|EMBL:KRZ50984.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ50984.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ50984.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ50984.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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 -!- 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:KRZ50984.1}.
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DR EMBL; JYDW01000243; KRZ50984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1KUD2; -.
DR STRING; 6335.A0A0V1KUD2; -.
DR Proteomes; UP000054721; 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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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; 3.40.50.1000; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
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; PF00122; E1-E2_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:UP000054721};
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 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 328..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 943..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 971..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1061..1080
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1087..1108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1128..1146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 72..137
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 908..1160
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1240..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 143270 MW; 610C56289097AD2F CRC64;
MASSSNDPST VVGMDVQNVT SKINPRNGRL TTRDVCFMPN TAAVISKMLK KFKKKRKPNP
QDNVSEVERR LRANDRDYNE QFDYARNFIR TSKYNLFTFL PKNLFEQFQR LANFYFLILM
ILQLIPQISS LTSLTTILPL VAVLSLTAAK DAFDDLQRHR SDNQVNNRKS QVVRGGQVVE
EKWQNVRVGD VIRMENDNFV AADLLLLSTS EPHGLCYIET AELDGETNLK AKQALPETAA
MGDDLIQISN FDGDIQCEAP NNCLSSFQGR LIWKEKTYSL DNEKMLLRGC VLRNTKWCFG
VVIFAGRDTK LMMNSGKTFF KRTSLDRFLN VLIIGIVLFL LSMCMISAVL CGTWEWTTGK
NFQAFLPWDS FVEQHSTTTA TVVFIAFLVF FSYAILLNTV VPISLYVSVE IIRVCHSWWI
NWDENLYYAP MDTAAKSRTT TLNEELGQIQ YIFSDKTGTL TQNIMTFNKC SINGVLYGDM
PEQVEQDKVR GKGGAPRPIS FSDNKWADDK FVFYDHKLLK HTKQRLAAVD QYWRCLSLCH
TVMSEMKTNR LEYQAQSPDE AALTIAARCF GYVFLSRTPR SISVEVMGVE EEYELLWILD
FNNVRKRMSV IVKKNNKIQL YCKGADTVIL RRITASPTDH LYSTTQAHLD KFASDGLRTL
CLAYKEISLD YYEQWQKRCH EASLSLENRQ DKMDAIYDEI ETGMTLLGAT AIEDKLQDGV
PETIANLIAA NIKIWVLTGD KQETAINIGY SCRLLTVNLK EVFVVDGSKI DDVRFQLECI
EQQICLGNGN GNGDPIVVLA NDSNSSCNVV GHTSVDRLDG YALVVNGHSL VHALQPTLEL
QFLKVATACK AVICCRVTPL QKALVVSLVK RNQKAVTLAV GDGANDVSMI KTAHIGVGIS
GQEGMQAVLA SDFSIAQFRY LERLLLVHGR WSYYRMCKFL QYFFYKNFAF TLAHFWFAFF
CGYSAQTIYD PLFIACYNLF FTALPVIGVG VFDQDVSDKN SLRYPELYIP GQQNLYFNMR
IFTYSVLRGF FSSGVLFFIP YAALSENVDF GGKSSAQSMQ ALSFTIFTAL IVTVTAQIAL
DTAYWTLINH IFVWGSLAFY FFVALVYYEL LPFDVLHHNG YGTAMEMFVY PNFWLSILLI
VVLLMLPHIS VRFFWVDVFP SLSDRIRVKQ NLRRLQGRLS EVPLQSLTTA SSLRRRRAST
RSSYAFSHHP GFGEMITKGL NMRQWKNELK LSTVIETLRR SSSSINRDPS TTCSNDQQPN
L
//
