ID A0A498KFH1_MALDO Unreviewed; 1809 AA.
AC A0A498KFH1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=DVH24_018430 {ECO:0000313|EMBL:RXI06388.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI06388.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI06388.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI06388.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC ECO:0000256|RuleBase:RU004279};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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:RXI06388.1}.
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DR EMBL; RDQH01000328; RXI06388.1; -; Genomic_DNA.
DR STRING; 3750.A0A498KFH1; -.
DR Proteomes; UP000290289; Chromosome 2.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 16.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 2.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 14.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1598..1806
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1063..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 219..246
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1063..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1809 AA; 201492 MW; 393A119692AFEF67 CRC64;
MPYSTFRLNL SVTSPYNADF DGDEMNMHVP QSFETRAEVL ELMMVPKCIV SPQANRPVMG
IVQDTLLGCR KITKRDTFIE KDVFMNILMW WEDFDGKVPA PAILKPRPLW TGKQVFNLII
PKQINLQRTS AWHSESESGN ITPGDTLVRI EKGELLSGTL CKKALGTSTG SLIHVIWEEV
GPDAARKFLG HTQWLVNYWL LQNAFSIGIG DTIADAATME KINETISKAK NEVKDLISKA
QSKQLEAEPG RTMMDSFENK VNQVLNRARD DAGSSAQKSL DESNNLKAMV TAGSKGSFIN
ISQMTACVGQ QNVEGKRIPY GFIDRTLPHF TKDDYGPESR GFVENSYLRG LTPQEFFFHA
MGGREGLIDT AVKTSETGYI QRRLVKAMED IMVKYDGTVR NSLGDVIQFL YGEDGMDAVW
IESQKLDSLK MKKTEFDRTF TYELDDENWN PDYMLHEHVE DLKTIREFRN VFDAEVQKLE
TDRLQLGTEI AVTGDNSWPL PVNLKRLIWN AQKTFKIDFR RTSDMHPMEI VEAIDKLQER
LKVVPGDDQL SVEAQKNATL FFNILLRSTF ASKRVLDEYR LTREAFEWVI GEIESRFLQS
LVAPGEMIGC VAAQSIGEPA TQMTLNTFHY AGVSAKNVTL GVPRLREIIN VAKRIKTPSL
SVYLKPEANK TKERAKNVQC ALEYTTLRSV TQATEVWYDP DPTSTVIEED IDFVKAYYEM
PDEEVNPDKI SPWLLRIELN REMMVDKKLS MADIAEKINL EFDDDLTCIF NDDNAEKLIL
RIRIMNAEAP KGEMVDESAE DDVFLKKIES NMLTEMALRG IPDINKVFIK HGKVNKFDQN
EGFKAEQEWM LDTEGVNLLA VLCHDDVDAR RTTSNHLIEI LEILGIEAVR RSLLDELRVV
ISFDGSYVNY RHLAILCDTM TYRGHLMAIT RHGINRNDTG PMMRCSFEET VDILLDAAVF
AETDYLRGVT ENIMLGQLAP IGTGDCALYL NDEMLKNAIE LQLPSYMDGL DFGMTPSRSP
VSGTPYHEGM MSPNYLLSPN LRLSPISDAQ FSPYVGGMAF SPTSSPGYSP SSPGYSPSSP
GYSPTSPGYS PTSPGYSPTS PGYSPTSPTY SPSSPGYSPT SPAYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPAYS PTSPAYSPTS PAYSPTSPSY SPTSPSYSPT SPSYSPTSPS
YSPTSPSYSP TSPSYSPTSP SYSPTSPAYS PTSPGYSPTS PSYSPTSPSY NPQSAKYSPS
SAYSPSSPRL SPSSPYSPTS PNYSPTSPSY SPTSPSYSPS SPTYSPGSPL TSGVSPDYSP
SSPQYSPSAG YSPSQPARPL PSENRLIGTE KSRSSWPLHG RILIDYSMDQ GFPYSPAETA
KVRRRQMSVA EIQHGETTVE GKPKTGGLSD PRLGTIDRKI KCETCASNMA DCPGHFGHLE
LAKPMYHIGF MKTVLSVIRC VCFKCSKILA DEEDQKFKQA LRIKCPKDRL KQIVDACRTK
TKCEGGDDID VQGLESEEPV KKSHGGCGAK QPKFSLDGIK MIAEYKAQRK KKDDQEQLPE
PVDRKKTLTA ERVLNVLKRI SDEELQLLGF DPDYSRPDWM ILQVLPIPPL AVRPSMMMDT
SSKSEDDLTY QLGTIIRHND NLRRQERIGS PARIISEFAQ MLQFHITTYF DNELPGLPRA
TQRSGRPIKS ICSRLKAKGG RVRGNLMGKR VDFSARTVIT PDPNINIDEL GVPWSIALNL
TYPETVTPYN IERLKELVEY GPRPPPGKTG AKYIIRDDGQ RLDLRYLKKS SDHHLELGYK
ALLFHSNKF
//
