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}.
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; 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
//