ID   RNH1_CRIFA              Reviewed;         494 AA.
AC   Q07762;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ribonuclease H;
DE            Short=RNase H;
DE            EC=3.1.26.4;
GN   Name=RNH1;
OS   Crithidia fasciculata.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX   NCBI_TaxID=5656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C1;
RX   PubMed=8415705; DOI=10.1073/pnas.90.20.9350;
RA   Campbell A.G., Ray D.S.;
RT   "Functional complementation of an Escherichia coli ribonuclease H mutation
RT   by a cloned genomic fragment from the trypanosomatid Crithidia
RT   fasciculata.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9350-9354(1993).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC       regulatory site, or after substrate binding. {ECO:0000250};
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR   EMBL; L18916; AAA03546.1; -; Genomic_DNA.
DR   PIR; A48683; A48683.
DR   AlphaFoldDB; Q07762; -.
DR   SMR; Q07762; -.
DR   VEuPathDB; TriTrypDB:CFAC1_220025400; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.40.970.10; -; 1.
DR   InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF01693; Cauli_VI; 1.
DR   Pfam; PF00075; RNase_H; 2.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55658; SSF55658; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN           1..494
FT                   /note="Ribonuclease H"
FT                   /id="PRO_0000195436"
FT   DOMAIN          272..488
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   REGION          79..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         281
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         281
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         325
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         480
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
SQ   SEQUENCE   494 AA;  53704 MW;  3E097DD1F376BE78 CRC64;
     MRRVALSVLF QSSRVLHFTD LRDKQIALCN AAPGHTVQFH QHRRHSSAPV SSVGGQNTFS
     CLGASCAGLL HPSRVRFANR RRSGSTSKKA QVKSSVNQLA IPSAATRERR KPKLSNSCAP
     AVESQKVGVA PTTSRASGET RTSCAPPPAS RMKPSFYVVA VGRQRGIYST WDQCSEQVKG
     FSGAVYKSFR TLSEARAYLT AHPARSGLEK SDRGDGAASL SALSEPQVGL RRSRAAEAEA
     SYVVEAPAQP TLRQRVEEEV PSGAAAVQRA ESSVPQVVYV DGACSHNGTP KARAGYGGFY
     GSTSDSRNFS LPVPITEAQT NNRGEMRAVI HCIVQGFVDA GVPPAALGTS HCVEPDWELS
     ELPQPLRRLV IYTDSRYVID GLTRYALKWV ANGFKLASKE PVLNQDLWRQ LIRLRDAYNT
     RYAEQQHWAA ATCSHASTRV PAASQSKRFH THNTRNDETE GIELRHVKGH SNDYGNEMAD
     VLAVAGARMH GTSE