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Database: UniProt
Entry: C4YSL5_CANAW
LinkDB: C4YSL5_CANAW
Original site: C4YSL5_CANAW 
ID   C4YSL5_CANAW            Unreviewed;       465 AA.
AC   C4YSL5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE            EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN   ORFNames=CAWG_05083 {ECO:0000313|EMBL:EEQ46718.1};
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ46718.1, ECO:0000313|Proteomes:UP000001429};
RN   [1] {ECO:0000313|EMBL:EEQ46718.1, ECO:0000313|Proteomes:UP000001429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1 {ECO:0000313|EMBL:EEQ46718.1,
RC   ECO:0000313|Proteomes:UP000001429};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|ARBA:ARBA00005300}.
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DR   EMBL; CM000312; EEQ46718.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YSL5; -.
DR   PaxDb; 5476-C4YSL5; -.
DR   VEuPathDB; FungiDB:CAWG_05083; -.
DR   HOGENOM; CLU_587919_0_0_1; -.
DR   OMA; QGHANIE; -.
DR   Proteomes; UP000001429; Chromosome 6.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   CDD; cd09280; RNase_HI_eukaryote_like; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 2.
DR   InterPro; IPR009027; Ribosomal_bL9/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   PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR   PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR   Pfam; PF01693; Cauli_VI; 2.
DR   Pfam; PF00075; RNase_H; 2.
DR   SUPFAM; SSF55658; L9 N-domain-like; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50879; RNASE_H_1; 2.
PE   3: Inferred from homology;
FT   DOMAIN          51..218
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   DOMAIN          284..451
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
SQ   SEQUENCE   465 AA;  53830 MW;  DF01D080E979D3C1 CRC64;
     MPYYAVVNGR EEGVFSSWQD CRPHVFAYKG AHFRKFEIRN EAEEYYQNDG DYFIYPIYVD
     GACRYNGCPH AEAGYGVYYG DGDSRNVSVP LDDVDPDGII PTNQRAELWA MNHALRNIWN
     ELQEDTEDGK AVIYSDSIYA IKCLTKWPNK WTQNGWLNVH GQTISNYDLV TKNYELYEWI
     NDEYDDRGWG ELDLIHVKGH SGNDGNEEAD NLANLAADRY GYQSSSSSSV WTIMPYYAVA
     RGREVGIYSS WRECRPQVYC CKGARYRKFE NLIEAKEYCE NDGRYYIYPV YVDGACRNNG
     RENAKGGYGV YYGDEDPRNV SVPLDRVDPN GIRPTNQRAE LWAMNHALKN ILNELQDETE
     KGKAIIYSDS IYAINCLTKW PEKWIYNGWQ NSRGRTISNQ ELIEENYDLY ESINEEYDDR
     DWGSLRFVHV KGHSGVEGNE EADRLANLAV DEYGQRSIFR SIFGF
//
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