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Database: UniProt
Entry: A0A0M3AHD6_9SPHN
LinkDB: A0A0M3AHD6_9SPHN
Original site: A0A0M3AHD6_9SPHN 
ID   A0A0M3AHD6_9SPHN        Unreviewed;       778 AA.
AC   A0A0M3AHD6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Haloacid dehalogenase {ECO:0000313|EMBL:KKW89502.1};
GN   ORFNames=YP76_24960 {ECO:0000313|EMBL:KKW89502.1};
OS   Sphingobium chungbukense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW89502.1, ECO:0000313|Proteomes:UP000033874};
RN   [1] {ECO:0000313|EMBL:KKW89502.1, ECO:0000313|Proteomes:UP000033874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ77 {ECO:0000313|EMBL:KKW89502.1,
RC   ECO:0000313|Proteomes:UP000033874};
RA   Kim Y.-C., Chae J.-C.;
RT   "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT   chungbukense DJ77.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell 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|ARBA:ARBA00006024,
CC       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:KKW89502.1}.
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DR   EMBL; LBIC01000020; KKW89502.1; -; Genomic_DNA.
DR   RefSeq; WP_046766091.1; NZ_LBIC01000020.1.
DR   AlphaFoldDB; A0A0M3AHD6; -.
DR   STRING; 56193.YP76_24960; -.
DR   PATRIC; fig|56193.3.peg.5270; -.
DR   Proteomes; UP000033874; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd02094; P-type_ATPase_Cu-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   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR045800; HMBD.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR011017; TRASH_dom.
DR   InterPro; IPR007029; YHS_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF19335; HMBD; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF04945; YHS; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00746; TRASH; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 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   Cell membrane {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   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        122..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        225..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        407..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        723..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        748..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          19..57
FT                   /note="TRASH"
FT                   /evidence="ECO:0000259|SMART:SM00746"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  81903 MW;  0D94E7F89DFFE10E CRC64;
     MDHARHDHDT LMGEQDARDP VCGMTVDPHG TAHRAGHGGK TYYFCSSKCQ ARFVADPLRF
     IGETSFSPNA NPEGTIWTCP MHPEVRQDHP GACPICGMAL EPEMARVESG PSPELADMTR
     RFWIGLILAF PVLVLEMGGH LFPALHHTVP MPVSIGIQLV LATPVVLWAG WPFFERGWTS
     LKTRSLNMFT LIAMGTGVAW AYSMVAALAP RLFPPAFRNA DGTVAVYFEA AAVITVLVLL
     GQLLELRARE RTSGAIKALL RLAPKTARRL LANGEDEEVS LDLVGVGDRL RVRPGEKVPV
     DGTVEDGRSS LDESMVTGES MPVTKIKGDS VIGGTLNQTG ALVIVATKVG RDTMLARIVQ
     MVAEAQRSRA PIQRMADQVS GWFVPVVVAI AALAFAGWGI WGPEPRFAYG LVAAVAVLII
     ACPCALGLAT PMSIMVGVGR GAGLGVLIKN AEALEHMEKV DTLVIDKTGT LTQGRPAVTA
     IVPAESYVEA DLLRFAASVE RASEHPLALA IVEAARSRSM ALPEVNAFDS PTGRGATGIV
     EGRRIVLGNA RFLGDEGIDT SALAASADDL RRDGATAIFL GIDGKAAGVI AVADPVKPTT
     PEALAALREA GIRVVMLTGD NKTTAQAVAA RLGIDEVEAE VLPDQKSAVI ARLKSEGRIV
     AMAGDGVNDA PALAAADVGI AMGSGTDVAI ESAGVTLLKG DLNGIVRARL LSRATMSNIR
     QNLVFAFIYN AAGVPIAAGL LYPLFGILLS PMIAAAAMAL SSVSVVTNAL RLNRQALR
//
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