ID A0A176VVL3_MARPO Unreviewed; 1024 AA.
AC A0A176VVL3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=AXG93_1217s1280 {ECO:0000313|EMBL:OAE23916.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE23916.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE23916.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE23916.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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:OAE23916.1}.
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DR EMBL; LVLJ01002730; OAE23916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VVL3; -.
DR OrthoDB; 317296at2759; -.
DR Proteomes; UP000077202; 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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF22; COPPER-TRANSPORTING ATPASE PAA1, CHLOROPLASTIC; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 557..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 600..623
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 921..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 954..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 194..271
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 976..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 106811 MW; 8631EC031DFA0078 CRC64;
MRQMGLLATD LAVQAPCLCT GLAAQGLTTL IPTNASRPWQ RQEPSNLLSL GLRLALARNG
LRVGMQAVQG LRVPITNKFS PPLGDAWLWR TNSALRIAPG SRSVGQLRHF VDAVKNSALC
HQCHAKLPTG ALACLSSTVN TFGGGGGRGY AGKGGGGGGG GGGDGFGAAA SKGAAAVGGE
QSDDVPFGGE VADDVIILDV GGMSCGGCSA SVKRILESQP QVTLANVNLA TETAFVQVVR
GSQPSPEWKT AKHAIGEALA KHLSSCGFKS TVRDLNTDSG KPSFVRKREE RIARLKDSGR
RLAVAWTLAA ICLVGHASHF VMNVLPPWAH FFHSTGFHMG LSLVALVGPG RKLLVDGWES
FKRRSPNMNT LVGLGAVSSF AVSTAAVLLP KLGWQAFFEE PVMLLAFVLL GRAVEERAKL
QASSDMTAIL NFLPTKARLI VNNGGDASRT MEVPAESLSI GDAVMVLPGD RIPVDGVVRG
GKSTVDESSL TGEPLPVLKE IGDEVSAGTV NYNGTLSVEA RRPGGETVLG DIVRMVEDAQ
TRQAPVQRLA DEVAGKFCYG VMALSGATFA FWSTLGQQLF PAVVPAGSAV LLGLQLACNV
LVIACPCALG LATPTAVLVG TSLGARKGLL IRGGDILEKI STLDTIVFDK TGTLTIGRPV
VTKVIPTTSK DDSILDGISG MNWSENELLA LAAGVERSTT HPIAKALVQA AAAADCRYAE
VKDGTFEQEP GSGAMAIVEG KRVTVGTTEW LQRHGAFGSP PEDLEASLEG QSVIYIGVDN
QLAGSVTMMD EIREEAVATV TALRMMGIQT SMLSGDKQAA AEAVAAKVGI PKDQVFAGVK
PKGKAEYIMQ LQREGKKVAM VGDGVNDAAA LAQSEVGIAM VGGVGAASEV ASVVLMGDKL
SQVVDAMELS RATFRKIKQN LWWAFMYNII GIPVAAGVLL PITNTMLTPS LAGALMGISS
IGVMANSLAL HLESNKFSSS GKTPSKSPPP YILNPRADYV VDVSKDTEDS KSDLEKSLLP
SPSK
//
