ID F6QPH0_CIOIN Unreviewed; 294 AA.
AC F6QPH0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ribonuclease H1 {ECO:0000256|PIRNR:PIRNR036852};
DE Short=RNase H1 {ECO:0000256|PIRNR:PIRNR036852};
DE EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR036852};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000025561.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000025561.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|PIRNR:PIRNR036852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR036852};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR036852};
CC -!- SIMILARITY: Belongs to the RNase H family.
CC {ECO:0000256|ARBA:ARBA00005300, ECO:0000256|PIRNR:PIRNR036852}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EAAA01001060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6QPH0; -.
DR STRING; 7719.ENSCINP00000025561; -.
DR Ensembl; ENSCINT00000025807.2; ENSCINP00000025561.2; ENSCING00000014054.2.
DR GeneTree; ENSGT00390000003466; -.
DR HOGENOM; CLU_030894_0_2_1; -.
DR InParanoid; F6QPH0; -.
DR OMA; ELWYGLY; -.
DR TreeFam; TF313356; -.
DR Proteomes; UP000008144; Chromosome 12.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR CDD; cd09280; RNase_HI_eukaryote_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR017067; RNase_H1_euk.
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 PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF00075; RNase_H; 1.
DR PIRSF; PIRSF036852; Ribonuclease_H1_euk; 1.
DR SUPFAM; SSF55658; L9 N-domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|PIRNR:PIRNR036852};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR036852};
KW Magnesium {ECO:0000256|PIRNR:PIRNR036852};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR036852};
KW Nuclease {ECO:0000256|PIRNR:PIRNR036852};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 144..290
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 90..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 32906 MW; 9A958DF9345D6E9C CRC64;
FTTCVYSVML RCCIRTAIMK SFYAVHIGKS PGVYDTWPEC LAQVSKFKGA KYKKFSNKDE
ASYFAHTGTE LSKDKSDILD IFKDELADNS AKESKPNNIP QSSIVSRKRK VKPDSNSRFG
KVQKTNDQPT NATHVVYLVA DSSDGSCPVV YTDGACSKNG RKGSRAGYGV WWGDDHKLNF
SARLPGIPTN QRAEIAAVNK AIKQAIDVGH KQLLIRTDSK FVIDCITKWV QGWIRKGWVK
ADGKPVIHKV EFQEMLKNMK KINVKFEHVF GHRGNYGNEM ADKLAVQGAT MPYL
//
