ID A0A2N5SXU8_9BASI Unreviewed; 347 AA.
AC A0A2N5SXU8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=HIT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PCANC_04720 {ECO:0000313|EMBL:PLW56159.1}, PCANC_14721
GN {ECO:0000313|EMBL:PLW18052.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW18052.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW18052.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW18052.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208}.
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:PLW18052.1}.
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DR EMBL; PGCJ01000838; PLW18052.1; -; Genomic_DNA.
DR EMBL; PGCJ01000024; PLW56159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5SXU8; -.
DR STRING; 200324.A0A2N5SXU8; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR Gene3D; 3.30.200.40; Scavenger mRNA decapping enzyme, N-terminal domain; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; HISTIDINE TRIAD HIT PROTEIN MEMBER; 1.
DR PANTHER; PTHR12978:SF0; M7GPPPX DIPHOSPHATASE; 1.
DR Pfam; PF05652; DcpS; 1.
DR Pfam; PF11969; DcpS_C; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT ACT_SITE 273
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 264..275
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 347 AA; 40325 MW; 81EECEBD4F7B73CC CRC64;
MQTEQTSRRV EELLRLFRFE RVINEDPSHH TINLLGTIET GSDDAASETR PEGELALAKT
SNKKAIMIIN KTHFPSQLEI LESINSPEQI KNIKTIGQND VYFWSLAWLN PFRPSLENTP
DLKISMIFPA TEVHIRKYTK QVNKIIRESP ELYQQVVLPY IKRIPPTRLS WLYNILDHVT
ESDKVVYEDP SESDGFMIIP DLKWDQTTIS SLYLLCIVRN REIYSLRDLC PSHLAMLKAI
RSSASESIEN KYNVPKRELR MFVHYQPSYY HFHVHITHVN HLGFQGITVG QAHLLDEIID
NLELEVKLTQ QTGTNHRSFY QSKTLTYALG SNHDLFEPLW SHQGLDK
//
