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Database: UniProt
Entry: A0A3M6VV82_9STRA
LinkDB: A0A3M6VV82_9STRA
Original site: A0A3M6VV82_9STRA 
ID   A0A3M6VV82_9STRA        Unreviewed;       215 AA.
AC   A0A3M6VV82;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   RecName: Full=HIT domain-containing protein {ECO:0000259|PROSITE:PS51084};
GN   ORFNames=DD237_002269 {ECO:0000313|EMBL:RQM10706.1}, DD238_002495
GN   {ECO:0000313|EMBL:RMX69676.1};
OS   Peronospora effusa.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Peronospora.
OX   NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX69676.1, ECO:0000313|Proteomes:UP000282087};
RN   [1] {ECO:0000313|Proteomes:UP000282087, ECO:0000313|Proteomes:UP000286097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R13 {ECO:0000313|EMBL:RQM10706.1,
RC   ECO:0000313|Proteomes:UP000286097}, and R14
RC   {ECO:0000313|EMBL:RMX69676.1, ECO:0000313|Proteomes:UP000282087};
RA   Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA   Reyes Chin-Wo S., Mou B., Michelmore R.;
RT   "Comparative genomics of downy mildews reveals potential adaptations to
RT   biotrophy.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RMX69676.1}.
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DR   EMBL; QLLG01000017; RMX69676.1; -; Genomic_DNA.
DR   EMBL; QKXF01000554; RQM10706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6VV82; -.
DR   STRING; 542832.A0A3M6VV82; -.
DR   VEuPathDB; FungiDB:DD237_002269; -.
DR   Proteomes; UP000282087; Unassembled WGS sequence.
DR   Proteomes; UP000286097; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd01275; FHIT; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   InterPro; IPR039383; FHIT.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR001310; Histidine_triad_HIT.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   PANTHER; PTHR46243; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR46243:SF1; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   Pfam; PF01230; HIT; 1.
DR   PRINTS; PR00332; HISTRIAD.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282087}.
FT   DOMAIN          66..173
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           158..162
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601310-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        160
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601310-1"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            178
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   215 AA;  24337 MW;  16F4AE4A15C77838 CRC64;
     MAASKKLEVP LHRTLLVTES TLLEDVANDV ILVTLPLQST DTKSHPFLVQ FVKDLLNFDQ
     CLDPTGRCFG PFRVPFTQIF YESELSFALV NLKPIVPGHV LVVPKRPVPR FEMLDVDEVS
     DLWNTAQLVG KQVERHYGAS SLTFAIQDGK EAGQTISHVH IHIIPRIAQD FKCNDDIYTK
     IEKHEQTLYV DNEMRTARSE SDMAAEAALL RPYFS
//
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