ID A0A498SDA0_ACAVI Unreviewed; 376 AA.
AC A0A498SDA0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC10 {ECO:0000256|ARBA:ARBA00020093};
DE EC=3.6.1.59 {ECO:0000256|ARBA:ARBA00012520};
DE AltName: Full=Decapping scavenger enzyme {ECO:0000256|ARBA:ARBA00030609};
DE AltName: Full=RNA polymerase III subunit C11 {ECO:0000256|ARBA:ARBA00029985};
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS {ECO:0000256|ARBA:ARBA00029885};
DE AltName: Full=m7GpppX diphosphatase {ECO:0000256|ARBA:ARBA00015636};
GN ORFNames=NAV_LOCUS2588 {ECO:0000313|EMBL:VBB27758.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB27758.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB27758.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616;
CC EC=3.6.1.59; Evidence={ECO:0000256|ARBA:ARBA00024271};
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208}.
CC -!- SIMILARITY: Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000256|RuleBase:RU003474}.
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DR EMBL; UPTC01000281; VBB27758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498SDA0; -.
DR STRING; 6277.A0A498SDA0; -.
DR Proteomes; UP000276991; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd10509; Zn-ribbon_RPC11; 1.
DR Gene3D; 2.20.25.10; -; 1.
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; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR InterPro; IPR034014; Zn_ribbon_RPC11_C.
DR InterPro; IPR001222; Znf_TFIIS.
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 Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|RuleBase:RU003474};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003474};
KW Reference proteome {ECO:0000313|Proteomes:UP000276991};
KW Transcription {ECO:0000256|RuleBase:RU003474};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00472}.
FT DOMAIN 333..375
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
SQ SEQUENCE 376 AA; 43290 MW; 541B07F261BDF83D CRC64;
MNTSVATEKT GNTGNNTINL ESFRFKEILG EDAAHKVAFV LLDVKGYGNQ AIMIAERTPF
PKNEQDWNTI VSHCSLKAVS TNDIYSNLIL FPPEKFAGIK ATLINPCTEK HITKYRDQKR
YVIHETPDDY KSITLPYLEE HQFTLKWIFN LLEHKAEVDR IIFDDTDPQN GFVLALDIKW
DGKNLENLYV LAIIRRKGIK SIRDLTVNDL PLLENISQKS YTAITEKYGI DKHQIRAYFH
YQPTFYHLHV HFIHVSYDAP ASGVAMKYML LFCPECGSSL QVEEGSNCYQ FSCHNCPYVQ
PITKLIKSRH YPKLKDLDEV LGGPGAWENA QITDERCPRC AGSRAYFMQL QTRSADEPMT
IFYRCANSEC AHRWKE
//
