ID A0A077Z913_TRITR Unreviewed; 1018 AA.
AC A0A077Z913;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=m7GpppX diphosphatase {ECO:0000256|ARBA:ARBA00015636};
DE EC=3.6.1.59 {ECO:0000256|ARBA:ARBA00012520};
DE AltName: Full=Decapping scavenger enzyme {ECO:0000256|ARBA:ARBA00030609};
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS {ECO:0000256|ARBA:ARBA00029885};
GN ORFNames=TTRE_0000497301 {ECO:0000313|EMBL:CDW56691.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56691.1};
RN [1] {ECO:0000313|EMBL:CDW56691.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW56691.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; HG806068; CDW56691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z913; -.
DR STRING; 36087.A0A077Z913; -.
DR GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 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; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
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 Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 265..657
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 1018 AA; 117168 MW; 80A2B7E1B21F0D62 CRC64;
MVNQQDGTHL IKHLHPTIIR NMVCSLPEIP DATVETNALM RTAPSNELPP FKSLTLRECL
DGSAKMALEF ESWIRTHCQK LSEANKLDLD FRNVVEEVEM RLAPVQYAGG TCRLLAGVMH
FHPNIIPRLR GVRLCVNSAK CHFLKKKFSY KTCCPEAGRR QLAEKTSMNE SQKALLSKYI
MEFKLNGLEM SDKKKRLWVE EYRRRLFDTY SLVDIQIFAV SILRRNGRLY FRFRPIRIIP
FCVTVVSGLP EGPFGNCSIV ALDSRKKLQG LATTFGYDCY ASMALHGRMA KSVDDVENMI
VSLKDAVSPK FADQCKGMTD LAASVDFLRP PLRPWDVDYY ARKLAEMKYG YTRYFLLDFI
DCIQFYRVSF NTISEYFPCS HVMPALLKLL EDMFDVQFLD AGEKAERWSD MVNVTVVGYT
PIVYVHLNLS SSNIRGEKPA LFHWDHLINF FREIGRSLQL LLTRMPFWEL ASGETLERDC
VMVVPYVLEN LLMQPQHLSA ISAHYSTGAK LSLEEALNFR KAIQAAQLPM LVRDIFKSDF
DLLIHKSNMG FWFDMYREKS KEYFPFGWEK GDYHPCNDLL VADDQAAASN YKQLWSEVVA
CDLLQAMGVV SKGTDQASVR QFCDSRKKTM LRFKRCYLAT DGSLTQSETF RRFTGRSLPS
VNGMLNMRFL LSNVEMEKST PDDNVLSDFE ILKVLKSDDD MKLIAVQARK RPRNELNAND
DGSQDAVVVL EKKPFTEETV AAFASDSSTR LTTVMHNDIY SVFNGTNADK VLLFTLWSHA
SELNGKPLIV PIICVRLCQL FDAAVKVTTI YPATAEHIRK WSEQPFFMVS ETPEDYKQTT
EPYILKNKLS LEWVYALLGG KAEAERVIYN DEDAVNGFIL APSLRWDGVR KEQMDLTAIV
RRRDLKSIRD LRADHLPLLY NLWAKCTTTI KEKYNVEANE MRIYFHYQPT YYHLHVHFTY
LKEWNIGTAA GRAHLFADVV QNLQTDGDYY AKRTMYFTLR EDDPLLTLLG RRNAFIRQ
//
