ID A0A1Y2EQN2_9BASI Unreviewed; 488 AA.
AC A0A1Y2EQN2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DHHA2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCR35DRAFT_306970 {ECO:0000313|EMBL:ORY73858.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY73858.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY73858.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY73858.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:ORY73858.1}.
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DR EMBL; MCGR01000044; ORY73858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2EQN2; -.
DR STRING; 106004.A0A1Y2EQN2; -.
DR InParanoid; A0A1Y2EQN2; -.
DR OrthoDB; 1342473at2759; -.
DR Proteomes; UP000193467; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR PANTHER; PTHR12112:SF20; -; 1.
DR PANTHER; PTHR12112; BNIP - RELATED; 1.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..488
FT /note="DHHA2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012824595"
FT DOMAIN 102..266
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 313..482
FT /note="DHHA2"
FT /evidence="ECO:0000259|Pfam:PF02833"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..328
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 488 AA; 53796 MW; 346BE3B9CB244CFD CRC64;
MLPLQLSSAL VALCALLPTS AALPSLPQQQ TFGEDARAFA PLSADPAFDV TKYKDGGPPS
PFPPSPTPGN ETGHGHFSIW SRETKEEFLR DVSSNSAQDW TLVMGNEAGD LDSMVSALAL
AYTLSHDSKN PQKAVALLQT EQDALYLRPE NALALHYARM ATHHRDLLTI DELPVKPSEM
WHRIKGIALV DHNVPLSRWG NATVLAILDH HEDRGHAPKA HPRVIEPSGS CSSLIARYMF
ERLDTIKKNG AEVLHGKLPT ELLELLLRTI AIDTSGLKKE QRQPVDKESA ETLFELSSWK
KGKLKKKMGE IDDELSKAKK NLADLDVRAL LRRDWKGDAV ETASTKYPAL ALGFASSPVS
LEEQILRTPE GTSPEWFAIE RAWTSEIGAD VSVCLTNFRD DDGTKTREIA LVVAHGFGKR
LSTRAATSLF DALKHAIENA GVELSPWSRP DGKPLLPRRG VWQLGEGSEA SRKFWRPIIE
KAAREWSG
//