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Database: UniProt
Entry: A0A139H1M2_9PEZI
LinkDB: A0A139H1M2_9PEZI
Original site: A0A139H1M2_9PEZI 
ID   A0A139H1M2_9PEZI        Unreviewed;       507 AA.
AC   A0A139H1M2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DHHA2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_2779 {ECO:0000313|EMBL:KXS96370.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXS96370.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXS96370.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXS96370.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXS96370.1}.
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DR   EMBL; LFZO01000834; KXS96370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139H1M2; -.
DR   STRING; 113226.A0A139H1M2; -.
DR   Proteomes; UP000073492; 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:UP000073492}.
FT   DOMAIN          124..289
FT                   /note="DDH"
FT                   /evidence="ECO:0000259|Pfam:PF01368"
FT   DOMAIN          333..499
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|Pfam:PF02833"
FT   COILED          320..347
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   507 AA;  57427 MW;  6B07E0E4F428F550 CRC64;
     MISLSEPNAV AYHAYCRALA QGGDRQGKHE TERQERVVQE ARLNAQHHLA LSFHVPYLLL
     LHSFLAAPSK HRHQAQAQAP LQPSRIQPAN AIETGVGHFS EWSRATKKEF LIDWQKGSIS
     EWTIVQGNEG GDLDSMVAAL TWAYHLEHST QNTSRPIKAI ALLQTPTDAL DLRPENKLAL
     QNAKMSTGHS DLLTLDELPE DPDTLARDLK GIVIVDHPKP LRKWGAAPIL SIFDHHQDAG
     AGKDAEPRVF EKVASCTTLV ARQMLDELEQ LPEEYHLPHE MLELILGAIA IDSGGLEDEN
     TTNEDLRTAS RILKRSRWSD RKLEKAMQDL DEKLSDAKKD LDDLNVRDLL RRDWKGDYVD
     TPSPQTPTVM LGFSSIPYSL DSQILKTEFK ELFDWFAIEA AWTAQEGTDI SIALNKYKVK
     DKKTGEKHKI REIVLVVRSD VRIDEVQADA LFKTVSEAIE KDPTLNAKPW HRVDELGRRQ
     MVWTHEREDA GRKVIRPIIE RAVESWD
//
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