ID K9G7M1_PEND1 Unreviewed; 428 AA.
AC K9G7M1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE RecName: Full=Ribonuclease H2 subunit B {ECO:0000256|ARBA:ARBA00019062};
DE AltName: Full=Ribonuclease HI subunit B {ECO:0000256|ARBA:ARBA00033464};
GN ORFNames=PDIP_29180 {ECO:0000313|EMBL:EKV17940.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV17940.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that
CC specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA
CC replication, possibly by mediating the removal of lagging-strand
CC Okazaki fragment RNA primers during DNA replication. Mediates the
CC excision of single ribonucleotides from DNA:RNA duplexes.
CC {ECO:0000256|ARBA:ARBA00024778}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV17940.1}.
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DR EMBL; AKCU01000194; EKV17940.1; -; Genomic_DNA.
DR RefSeq; XP_014536379.1; XM_014680893.1.
DR AlphaFoldDB; K9G7M1; -.
DR GeneID; 26231238; -.
DR KEGG; pdp:PDIP_29180; -.
DR HOGENOM; CLU_057573_0_0_1; -.
DR OrthoDB; 2100348at2759; -.
DR Proteomes; UP000009886; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IEA:InterPro.
DR CDD; cd09270; RNase_H2-B; 1.
DR Gene3D; 1.10.20.120; -; 1.
DR InterPro; IPR040456; RNase_H2_suB.
DR InterPro; IPR019024; RNase_H2_suB_wHTH.
DR InterPro; IPR041195; Rnh202_N.
DR PANTHER; PTHR13383; RIBONUCLEASE H2 SUBUNIT B; 1.
DR PANTHER; PTHR13383:SF11; RIBONUCLEASE H2 SUBUNIT B; 1.
DR Pfam; PF09468; RNase_H2-Ydr279; 1.
DR Pfam; PF17745; Ydr279_N; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 34..125
FT /note="Rnh202 triple barrel"
FT /evidence="ECO:0000259|Pfam:PF17745"
FT DOMAIN 128..326
FT /note="Ribonuclease H2 subunit B wHTH"
FT /evidence="ECO:0000259|Pfam:PF09468"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 47663 MW; 661FFB0FB0C33183 CRC64;
MKTRSASVSK VQKSEDETKT KPLVAAEKPS KTFILPSSTS DNARLLSLPD PQSGELKRYF
FCPNRGIYEF TVVSPPAHLA RSILFIPRTR ETASPSEEEK KDPEKLSAQG SITKKAEFLM
ATPIDALFFM VPLLAPSSKS GRSLFQPFDD IIDSHDDMPH HLRQVLCDDE FRDSLLARTE
AICEVVEAGD EKMFRFNEMK LVQEFVAKAE RIADRGLPAS MEEHFVRQAL ATPLMSVKRE
DVATSQEPSN ESQEASKSEE RQDSLSTVDT AMTPSVASPA GELTPVSQPP SEESTASDHI
ARLLRISTAL SFMKESYLPA SMASKVDEIL ASAESPVDFE PLKDRLKQIA DLRATALASR
DMSNFSRKRD HDDEEEDTRA EKKRRKEEEE KKSKAAQSQA VKNLKKVNTS GMQKLSSFFA
KAAPKKKT
//
