ID X6NV02_RETFI Unreviewed; 930 AA.
AC X6NV02;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=HMA domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=RFI_07491 {ECO:0000313|EMBL:ETO29629.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO29629.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO29629.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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:ETO29629.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASPP01005941; ETO29629.1; -; Genomic_DNA.
DR AlphaFoldDB; X6NV02; -.
DR EnsemblProtists; ETO29629; ETO29629; RFI_07491.
DR OMA; KFGSMNM; -.
DR OrthoDB; 7279at2759; -.
DR Proteomes; UP000023152; 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 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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR Pfam; PF00122; E1-E2_ATPase; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 PROSITE; PS00154; ATPASE_E1_E2; 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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152};
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 152..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 315..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 545..567
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 719..740
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 358..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETO29629.1"
SQ SEQUENCE 930 AA; 104214 MW; 2A2880A76F0B7504 CRC64;
SNEVTIKISG LSSESSSKLR EKLLEYEGII SVKIHDQYNN KSSVPKQATN NCEDMWDALW
QRVQMKVWSG SLQERSIDAT AILEPDVEVD ASKVVYFAIA FDKEITGLRH IKAYIECQCG
LECHLLYDSM DITQRNLDMQ QNRAREQQKW KLLIGFSLFF SIPAFLLGMV LPLISKGFQT
AFAEQIVTGC SIGDLVMFLL VTPVQFGPPG LLFLRGAYKS LSKAKTANMD VLVTLATFTS
YFFSCISVLI CIADQAANSS QTMFDTSSTL ITVILLGKYM ETIAKGKTSE ALDKLMDLQV
RRFQKKKNCS HKIHTIIYII FFTFGFNLYT YMPTCLHAYI HISHLVTKYP SEWITKKREN
KEEEEEKKPM EEKEKEKKKK MKENPRLLQV GDIVEVKRGE KIPMDGVVVK GESQVDESLI
TGESLAVKKT VGDEVIGATV NVSTTLYFRV TKTGSETMLS KIIQLVESAQ TTKAPVQKLA
DNIATKFVPA VIFASTTVLI LWIMLFYYNV VHTQQLMGVM GDSQSNNESQ SHSMSSSSFT
IHSKVFYSVM FSISVLVISC PCALGLATPT AVMVGTGKAA EFGVLFKSGE PLERAGQVTC
IVFDKTGTLT QGKMQVVKVL MDCEKIHTLF TDKNNNARDA QHIKILTQWL WKMIYSCQCQ
SDHVIAHAIC TFFESIFPDQ KNTSLLCQSF EAQTGLGVHG VFHLSADPNS AAYEVNLNLF
YLFIYLFFET LLSVQISSIL KTDLTQYLTR LRKSGFTVVF VSLNRTLVCA IAVADTIKPE
SKQVIHTLQS MYHVDCWMIT GDHTLNSYVI ADQIGIHRSR VRAQVQPKDK QFIVQQLQKQ
YVHIHYHIEG EGKKRHIVAF VGDGINDSPS LAAADVGIAI GAGTDVAIAS ASVVLMRSNL
LDILEVITIS RLTLRKIWQN FGWALIYNVQ
//
