ID E3QRQ0_COLGM Unreviewed; 437 AA.
AC E3QRQ0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Ribonuclease H2 subunit B {ECO:0000256|ARBA:ARBA00019062};
DE AltName: Full=Ribonuclease HI subunit B {ECO:0000256|ARBA:ARBA00033464};
GN ORFNames=GLRG_08817 {ECO:0000313|EMBL:EFQ33538.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(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 ---------------------------------------------------------------------------
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; GG697371; EFQ33538.1; -; Genomic_DNA.
DR RefSeq; XP_008097558.1; XM_008099367.1.
DR AlphaFoldDB; E3QRQ0; -.
DR STRING; 645133.E3QRQ0; -.
DR EnsemblFungi; EFQ33538; EFQ33538; GLRG_08817.
DR GeneID; 24414182; -.
DR VEuPathDB; FungiDB:GLRG_08817; -.
DR eggNOG; ENOG502SAQ3; Eukaryota.
DR HOGENOM; CLU_057573_0_0_1; -.
DR OrthoDB; 2100348at2759; -.
DR Proteomes; UP000008782; 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 Gene3D; 2.20.25.530; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT DOMAIN 40..126
FT /note="Rnh202 triple barrel"
FT /evidence="ECO:0000259|Pfam:PF17745"
FT DOMAIN 129..342
FT /note="Ribonuclease H2 subunit B wHTH"
FT /evidence="ECO:0000259|Pfam:PF09468"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 47771 MW; 0B092C63FA47C52D CRC64;
MARTRSTKSA PAAKTEDTNA SLAAKHSLPE ESSSPPKLFI IPNKATKEAR IVSLPNPRYS
KLTRYLLCPD TGIYEFTKIA APKATPRSWL IETPAGNLER TGPTDGLRFE AHVTSGADLF
VATPFDPLFL LVPGLFGPTN AKTPDMKRLF LSSDDHFDAL STSSSHLSEA LRCHKTRALL
ESRMESISDT VDAGEEKMYR LSEKKLVLEI LSKARSMSSK GLPASMEEKF VKKALEAPIQ
VQKSQATAVK QAPETTTDEL STPASKNIPE ESQSSISIED SAAAAVSNAS TAATSVATEV
AEETVSSAIH ASDEVTSLQR LRIAFSFICS SYIATGMAAN LKELLEDKET SGVNFSPLDG
YLAQLTKLRA EAASSRSMGD YSRKRMLDEE EEELRAEKKR KMEEEKKKKA SQSRGVKALE
KVNTKGMKKM SDFFKKK
//