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Database: UniProt
Entry: A0A150V5A9_9PEZI
LinkDB: A0A150V5A9_9PEZI
Original site: A0A150V5A9_9PEZI 
ID   A0A150V5A9_9PEZI        Unreviewed;       321 AA.
AC   A0A150V5A9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=HIT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M433DRAFT_143689 {ECO:0000313|EMBL:KYG45726.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG45726.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG45726.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG45726.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG45726.1}.
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DR   EMBL; JPDO01000148; KYG45726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150V5A9; -.
DR   STRING; 766039.A0A150V5A9; -.
DR   Proteomes; UP000075602; 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:UP000075602}.
FT   ACT_SITE        249
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
SQ   SEQUENCE   321 AA;  37115 MW;  3CBF63270B4FA434 CRC64;
     MSNTSTSLIT RFKFISLHNQ DQGGRRIILR GTISGEPALL IAERGNFDTD PAYLASFSRL
     ITHVKSLGHN DVYRWYLANS LSENGIDQPT PPDLKLDLFY PATEKHLRKY AFQQYRVVTE
     TPEMYAKYVR PFIERSREGG RLDWIFNIVE GRAEQENVVY RSQEADKNDD FLLLPDLHWD
     RKTISDLHLL AVIVRRDIWS LRDLTKKHLP WLNHLRCTLA TTVTKLYPGV EEDLLKFYVH
     YQPTYYHFHI HVVHTNVEPG ITQAVGKARD FDSIISQLET MRGGEEAGMK DVSMRVTVGE
     ATELWTEVFL PLKEGRDPLV G
//
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