ID A0A0V1NZF0_9BILA Unreviewed; 873 AA.
AC A0A0V1NZF0;
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:KRZ89285.1};
GN ORFNames=T08_14454 {ECO:0000313|EMBL:KRZ89285.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ89285.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ89285.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ89285.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRZ89285.1}.
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DR EMBL; JYDM01000072; KRZ89285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NZF0; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000054924; 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 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:KRZ89285.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
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 873 AA; 98678 MW; A07F0AACF1F7FC44 CRC64;
MFWRYFTRAF HACTLNKVPY IPIVVEQTGR GERAYDIFSR LLEERIICVM GPITDELSSL
VIAQLLFLQS KSLTKPVHMY INSPGGSVTA GLGIYDTMQY IKPRILIATW CIGQACSMAS
LLLASGTEGY RNCLPNARVM IHQPSGQAVG QATDIMIQAE EIIKLKRQIN KLYVKHTKKP
YNVIEEAMER DLFMSPEDAA EFGLIDKIVN LGAGFDTLFF RLRKKYKEKI TRFLDVDLPS
VVKQKYAILN KYDSVFFPEA DKNSPNGGGT IQKSDEIFPF SSQYALVACD LRNNDELIAL
LLTGCRLCSM IPTLFIAECV LNYLNVNERK DASNVERKAV FLFYRSNRLL EMFPVIFNKC
SIISYEQVLP RDTFGRFMCE HFANVGSPLL SIDQYPDASS GIDRLNSLGW ENVTVYSLSS
IYYCSLSEQE RKRISELEEF DEYEMWHLKC SHYVIVVGST VSFFLHKYNK LFPISAMPLD
VLENSFFYRL KSVFGESSYM PAEVGQGFRM QVKAHVAHVA KQADEIKRVG LRCIPMGENV
ILIGGWGASA SGKHKRLASV CYWNVREDVV SVVEKKVTNF DPSDGRDPAE RMFHSVTAVE
DGQFVLFGGR TSPYNPMMDS WLCEITQTKM LKMEPVKIEK SKFRPVPRAR YRHAACCIDN
YFGRCVVFIC GGIGLETADG KAKNPQSLKV MDDCWILDYQ FQEWKQVANM PVSLHSHRCA
YVASNGTVVV VGGLESLDDR FSSALYFFST VSNCWTMKWR WSPSVDRYGF TAHLIGEEML
LLVGGVNRDH GECHDVALVS LNDGKAICLA IELEVKVERV ATDGFMFVNH DSVLIQNGDG
HILYILGGGG NCFSFGTLLN HHILRIDLPM LSF
//
