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Database: UniProt
Entry: Q6C6W2_YARLI
LinkDB: Q6C6W2_YARLI
Original site: Q6C6W2_YARLI 
ID   Q6C6W2_YARLI            Unreviewed;       907 AA.
AC   Q6C6W2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE            EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN   ORFNames=YALI0_E05775g {ECO:0000313|EMBL:CAG79181.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79181.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79181.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|ARBA:ARBA00005300}.
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DR   EMBL; CR382131; CAG79181.1; -; Genomic_DNA.
DR   RefSeq; XP_503600.1; XM_503600.1.
DR   AlphaFoldDB; Q6C6W2; -.
DR   EnsemblFungi; CAG79181; CAG79181; YALI0_E05775g.
DR   GeneID; 2912330; -.
DR   KEGG; yli:YALI0E05775g; -.
DR   VEuPathDB; FungiDB:YALI0_E05775g; -.
DR   HOGENOM; CLU_320089_0_0_1; -.
DR   InParanoid; Q6C6W2; -.
DR   OrthoDB; 3280806at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
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; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300}.
FT   DOMAIN          710..860
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          45..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          107..134
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        483..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  104259 MW;  BB11932950D8D8B9 CRC64;
     MSGFTTFHAM IRLRPLTIPI RIFIRNVSLS SGFRHQKYKR LDYPKAPTLL RDPPPEVRAV
     PQTPPETFSV KRQGRNKAGR KQTTEMYTFV SQKDALEFEL APSAVLRQTI EKRLASLSQE
     QRELKAEMET QIARAGGVFA VRKGLVPGIY LHWDKVVRET GKMSQSEWKK LETVQEAQEW
     MGMYHVSPED VCYDPFASRI SFLEHLLSDE AKLEPEKKRW FAVKKGRQPG VYSNWEEAAD
     QVIGYSGAVY ASFSTDKQAC KFLGMSKKEY FEQLKQDPTE TDKEMIRQKR LADEQLQAYK
     RERDRIKFSQ YAEAKMYIAP PDGGSPNRVK QLLTKCLQIQ AEINKMVSLD KMRKFHMQDI
     FDELDQMTEE EKQECLESLD NSHLVDAYNV FNNPEYWDFY REYLLTKENY LGYESTTCSK
     GRGDTLFKSE FRECGTTKST TEELAATEVS QWRQKNETSV ENDTVKLDTS SEGFFSSTQE
     LSERTEDTVD KKLTQRQKRD SKRATLKALD KSISENIAAP DDVAIGIKEN GTVRNQAKKT
     TFENWLDGFS EAEKHKPASK ITLTGHFKNA TPQMRREMLK ARHETKMELV ARTADPSTTV
     TLDMLAGLTC NCGEPVFVRN RDSSAAAPLI PRRQLYLSTN RYKNLHGDSG WTNHTFKHKQ
     ADFDINTTSF RDHHDHKLLR AFETNWRIMF NSLSKQLGPI AANHAGRYDD VEANVVYTDG
     SHNALPSPLL YNAGAAGWGV HFEKGLMPDA CGRVPGEQTP GRAEILAMVM AIRIISRHMT
     YRSQKWEIRT DSLWTLRLLE HGWEGLEPTE RMRSHPNYYL IKRLRALLYE NQNISLRFIR
     SQHMHSGARI ADKLAKKGAR KKYSETAEQY GTDDEDIFIH DPALSAFFPS ATVPSNLRSS
     MWTDNKE
//
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