ID A0A0G4N586_9PEZI Unreviewed; 1212 AA.
AC A0A0G4N586;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=HRDC domain-containing protein {ECO:0000259|PROSITE:PS50967};
GN ORFNames=BN1708_001803 {ECO:0000313|EMBL:CRK41475.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK41475.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK41475.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK41475.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC {ECO:0000256|ARBA:ARBA00043957}.
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DR EMBL; CVQH01026971; CRK41475.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4N586; -.
DR OrthoDB; 2880475at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:InterPro.
DR CDD; cd06147; Rrp6p_like_exo; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR045092; Rrp6-like.
DR InterPro; IPR049559; Rrp6p-like_exo.
DR PANTHER; PTHR12124:SF47; EXOSOME COMPONENT 10; 1.
DR PANTHER; PTHR12124; POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 2.
DR Pfam; PF08066; PMC2NT; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 2.
DR SUPFAM; SSF47819; HRDC-like; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50967; HRDC; 2.
PE 3: Inferred from homology;
KW Exosome {ECO:0000256|ARBA:ARBA00022835};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 16..96
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT DOMAIN 812..892
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 110..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 136034 MW; 1F388FD56E8A383C CRC64;
MRRHRGEGDW AYFRCTTSES TXYRAIWKWR DDTARRLDES TGYVLPNVAI AEIARHMPPD
AKALHSLIHS NSIIAKRNVG EIWAAFKKGR DEGDDSQSLL RFFQNDTSST TTTRRATQKL
SERTADVPDD VQSGKLDRSQ LFGDVPISSK WEASLTSRPQ GYVLLPWQRI MQEAGQKALS
TSEDVEMADK QPESAAPAAP AAPAQEEPDR EFTLRSGLKR KQVEEEEEES DSSSEDEDED
DKDSSDVEEA IEIEDEEAKL ERERKERKTA KLQRKAAKRA AKKAQAEAGE DELEESSDAK
TGRKSALQDQ NLLLLDLVAL GRKRGRHFEL GYRNGWKVDP LRYDFLTQPT SNSQSPTRSI
PSQLTTVTVA MASPDFKALQ DEVQKALVTT VKSANRIAAE DLAFQRTVNP SVADELDETT
ARLLGLSHKL LKSAAEVCGQ GSVPELEDAD DVDMHWRKIV DVLDNVLEKA DRSIDEFTGV
LKRKDAPTET TPNAKKPRTA LASNMRNANI AKPQLEFERA IDNTSWRPVL SKKPNASVPL
EESLAKDSAE SGSKHPYEAE ILAAKYPERV YQKAEPILYH PVKSTTAKWV DTYEGVLEML
GELKKAKEIA VDLEHHDTRT YAGLLSLMQI STRDQDWIVD TLKPWRHQLE VLNEVFTDPK
IVKVFHGAHM DMQWLQRDLG LYINGLFDTF FAAEILGYPQ RSLAYLLKRF VDFDADKKYQ
MADWRIRPLP EEMFYYARSD THYLLYIFDR IRNELLDASD RSKPETDIIQ QVLQKSKELS
LSRYEGLDFD PETGHGSRGW YGVLLKNPMP LSGKQFAAYR AIWKWRDDTA RRLDESTGYV
LPNAAIAEIA RHMPPDAKAL HSLIHGNSII AKRNVGEIWA AFKKGRDEGD DSQSLLRFFQ
NDTSSSTTTR RATQKLAERA ADVPDDVQSG KLDRSQLFGD VPISSKWEAS LTSRPQGYVL
LPWQRIMQEA GRKAPSTSED VEMADKQPES AAPAAPAAPA QEEPDREFTL RSGLKRKQVE
EEEEESDSSS EDEDEDDKDS SDVEEAIEIE DEEAKLERER KERKTAKLQR KAAKRAAKKA
QAEAGGDEPE ESSDAKTGRK SASASEPDFE GADKAEKKRK KLEKAERKAA KEAKKQAKAA
RKAEEEAAKA AAGAPEAFDY SNASSVLHAG RNAGGGVQKE RFDPYSKTGE DGPKGARKAP
PLHGNRSATF RK
//
