ID   TRHP_HAEIN              Reviewed;         460 AA.
AC   P44700;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=tRNA hydroxylation protein P {ECO:0000250|UniProtKB:P76403};
DE            EC=3.4.-.- {ECO:0000305};
GN   Name=trhP {ECO:0000250|UniProtKB:P76403}; OrderedLocusNames=HI_0419;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in prephenate-dependent formation of 5-
CC       hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first
CC       step in 5-carboxymethoxyuridine (cmo5U) biosynthesis.
CC       {ECO:0000250|UniProtKB:P76403}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22077.1; -; Genomic_DNA.
DR   PIR; G64066; G64066.
DR   RefSeq; NP_438581.1; NC_000907.1.
DR   RefSeq; WP_005693745.1; NC_000907.1.
DR   AlphaFoldDB; P44700; -.
DR   SMR; P44700; -.
DR   STRING; 71421.HI_0419; -.
DR   MEROPS; U32.002; -.
DR   EnsemblBacteria; AAC22077; AAC22077; HI_0419.
DR   KEGG; hin:HI_0419; -.
DR   PATRIC; fig|71421.8.peg.439; -.
DR   eggNOG; COG0826; Bacteria.
DR   HOGENOM; CLU_011540_0_2_6; -.
DR   OMA; YGGVSHF; -.
DR   PhylomeDB; P44700; -.
DR   BioCyc; HINF71421:G1GJ1-434-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR001539; Peptidase_U32.
DR   InterPro; IPR032525; Peptidase_U32_C.
DR   Pfam; PF01136; Peptidase_U32; 1.
DR   Pfam; PF16325; Peptidase_U32_C; 1.
DR   PROSITE; PS01276; PEPTIDASE_U32; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; tRNA processing.
FT   CHAIN           1..460
FT                   /note="tRNA hydroxylation protein P"
FT                   /id="PRO_0000079185"
SQ   SEQUENCE   460 AA;  52126 MW;  8FDC8FFDECD1C537 CRC64;
     MTTQFKPELL SPAGSLKNMR YAFAYGADAV YAGQPRYSLR VRNNEFNHAN LKIGIDEAHS
     LGKKFYVVVN IAPHNSKLKT FIKDLQPVID MKPDALIMSD PGLIMLVREN FPNIDIHLSV
     QANAVNWATV KFWKQMGLTR VILSRELSID EIAEIRQQVP DIELEIFVHG ALCMAYSGRC
     LLSGYINKRD PNQGTCTNAC RWEYKMEEGT TDDVGNIVPK IDPAQQIEVK NVAPTLGEGA
     VTDKVFLYTE SQKPDEQMTA FEDKHGTYFM NSKDLRAVQH VEKLTALGVH SLKIEGRTKS
     FYYCARTAQV YRKAIDDAAA GKPFDESLMD TLESLAHRGY TEGFLRRHTH DEYQNYEYGY
     SISDRQQFVG EFTGKRNEQG MAEVAVKNKF LLGDNVEMMT PQGNINFKIE KMLNRKNETV
     DAALGDGHFV FLNVPQDINL NYALLMRNLV NTNTRNPHSN