ID A0A0V1LHB5_9BILA Unreviewed; 875 AA.
AC A0A0V1LHB5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Endopeptidase Clp {ECO:0000256|PROSITE-ProRule:PRU10086};
DE EC=3.4.21.92 {ECO:0000256|PROSITE-ProRule:PRU10086};
GN Name=CLPP {ECO:0000313|EMBL:KRZ58905.1};
GN ORFNames=T02_11130 {ECO:0000313|EMBL:KRZ58905.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ58905.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ58905.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ58905.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in
CC tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-
CC homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119,
CC Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231;
CC Evidence={ECO:0000256|ARBA:ARBA00000401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-
CC adenosyl-L-methionine = 7-[(3S)-(3-amino-3-
CC methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-
CC COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543,
CC ChEBI:CHEBI:74275; EC=2.1.1.290;
CC Evidence={ECO:0000256|ARBA:ARBA00001806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000256|ARBA:ARBA00034021,
CC ECO:0000256|PROSITE-ProRule:PRU10086};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000256|ARBA:ARBA00010703}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family.
CC {ECO:0000256|ARBA:ARBA00007039}.
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:KRZ58905.1}.
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DR EMBL; JYDW01000050; KRZ58905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LHB5; -.
DR STRING; 6335.A0A0V1LHB5; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd07017; S14_ClpP_2; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR46529; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 4; 1.
DR PANTHER; PTHR46529:SF1; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 4; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF04072; LCM; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRZ58905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT ACT_SITE 117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10085"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10086"
SQ SEQUENCE 875 AA; 98931 MW; 088C656349EC5B8D CRC64;
MFWRYFTRAF HACTLNKVPY IPIVVEQTGR GERAYDIFSR LLEERIICVM GPITDELSSL
VIAQLLFLQS KSLTKPVHMY INSPGGSVTA GLGIYDTMQY IKPRILIATW CIGQACSMAS
LLLASGTEGY RNCLPNARVM IHQPSGQAVG QATDIMIQAE EIIKLKRQIN KLYVKHTKKP
YNVIEEAMER DLFMSPEDAA EGYYIRVHAI YKAVRIFIET SNFPVQIVNL GAGFDTLFFR
LRKKYKEKIT RFLDVDLPSV VKQKYAILNK YDSVFFPEAD KNSPNGGGTI QKSDEIFPFS
SQYALVACDL RNNDELIALL LTGCRLCSMI PTLFIAECVL NYLNVNESNR LLEMFPVIFN
KCSIISYEQV LPRDTFGRFM CEHFANVGSP LLSIDQYPDA SSGIDRLNSL GWENVTVYSL
SSIYYCSLSE QERKRISELE EFDEYEMWHL KCSHYVIVVG STVSFFLHKY NKLFPISAMP
LDVLENSFFY RLKSVFGESS YMPAEVGQGF RMQVKAHVAH VAKQADEIKR VGLRCIPMGE
NVILIGGWGA SASGKHKRLA NVCYWNVRED VVSVVEKKVT NFDPSDGRDP AERMFHSVTA
VEDGQFVLFG GRTSPYNPMM DSWLCEITQT KMLKMEPVKI EKSKFRPVPR ARYRHAACCI
DNYFGRCVVF ICGGIGLETA DGKVKNPQSL KVMDDCWILD YQFQEWKQVA NMPVSLHSHR
CAYVASNGTV VVVGGLESLD DRFSSALYFF STVSNCWTMK WRWSPSVDRY GFTAHLIGEE
MLLLVGGVNR DHGECHDVAL VSLNDGKAIC LAIELEVKVE RVATDGFMFV NHDSVLVQNG
DGHILYILGG GGNCFSFGTL LNHHILRIDL PMLSF
//
