ID A0A1X2IJ17_9FUNG Unreviewed; 311 AA.
AC A0A1X2IJ17;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=HIT-like domain-containing protein {ECO:0000313|EMBL:ORZ17326.1};
GN ORFNames=BCR42DRAFT_414395 {ECO:0000313|EMBL:ORZ17326.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ17326.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ17326.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ17326.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:ORZ17326.1}.
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DR EMBL; MCGE01000010; ORZ17326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IJ17; -.
DR STRING; 90262.A0A1X2IJ17; -.
DR OrthoDB; 5490768at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR019808; Histidine_triad_CS.
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.
DR PROSITE; PS00892; HIT_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 234..245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 311 AA; 35959 MW; 9491FCE3211D5291 CRC64;
MSALTTILKN FQYERVLSHN TRTKMIHLLG QVDGQACILS LEKLPYDDHA IPTLGQHVDT
LADEVENNIY GWGLGHIRLE HLDTQIKYIY PATDLHIRKY EDQQRYLIKE TPTVYDEVTR
PYINSIPATR IDWVHNILNG KAEVDRVLYH DKHEENGFVI LPDMKWDGHP DSLYLVAIVM
NPSLTSLRSL TTNHIPLLER IQSTSIKIAQ EQQQQSAATS DIITDPPQLR CFIHYQPSYY
HLHIHITALS MQDPPGAMVG QAHLLDSVID NLTLYPDYYQ KATLSYVIGE QHPLYSNYTT
WLKQQDKDKK Y
//
