ID A0A176VP21_MARPO Unreviewed; 1699 AA.
AC A0A176VP21;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AXG93_328s1100 {ECO:0000313|EMBL:OAE22658.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE22658.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE22658.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE22658.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {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:OAE22658.1}.
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DR EMBL; LVLJ01003102; OAE22658.1; -; Genomic_DNA.
DR OrthoDB; 455034at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02737; RNAP_IV_NRPD1_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 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; IPR040402; NRPD1_C.
DR InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF51; DNA-DIRECTED RNA POLYMERASE V SUBUNIT 1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
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 SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 437..750
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 139..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1699 AA; 188482 MW; 1173B69B4D063CBF CRC64;
MEVSEVPPEG GTPQLAKICG IQFGLMTTAN TLNMSVLVTR EGSIRSKDPM NAYFGLPTPS
GKCLTCNGVT VDECQGHFGH ILLSLPIFHP NYVEALVTLL RRICLNCGQL RKKSKLSSYH
ESSLALLAGA DHQAQSNLGT HSNYQSHEPK GTECNTSNPV HADIGMSSES NSRNKRKLEE
ALDEDIDDWP DGLKPCISPE EVIVLSSDDS DEDFSGKAKE LQGMETNCKT GQVTKCASPG
IPTSSRKMLR KRKTVSYTEE LNCKSPESEF AVPSKGSGSK AYKRRRTSME SRQTEKSRVI
LSGDTVEPAS KSVKFATKVC KYCSHGQSLN VGGSPQASSR RLGYPKPDIN VHVNLKGASN
EDPFNSVKFI KMSVKPKERE NLAADYWDFV EGSSKLEKPL KRGSRYLLPS EALNILKKIP
QKSITALGMK ANIACPEAMI LECLPVPPNC TRLQEDAFGK GGTNLGFKIG VDRATQAFER
LVRKINIIKT SRFGKPSFQA AVVECCVLQA LFQQYLREKG APKTAPGKEK KKVDTSGRLQ
HRPTRWSLDW LKKNLIGKRS GFSARNVVTG DPYLSVEEIG VPMDIAKHVT YSERVTDFNR
SRLQEYIDIG QDLGKSMACG AVRIIRKDER REVTRKTEID LQTGDIVHRH LKDGDLVFVN
RPPSLHKHSL LALKANIHSG ATWTINPAIC APLHADFDGD CLHVFVPQTE ESRAELHQLM
TIPAQILPSP DENTILGLSQ DYVLATYLVT SSPLFLPKDS MHQLAMWTKK QLPVPTIVKS
PKLGPLWTGK QVIDLAIPEG FSFQSNNGAT RIHDGEILSC GEKSNWLAST KGLVRIIAQK
NTDAAVEHID CSQAVLREWL LSQGFSVSLE DFYAAPDQDM RRKLKYKIED NLEHAQCMFV
CRGDKKILNI NTSSNASMSI LDSAAPSERR RRRHGLEDAA ISSFRQTQSQ IGETFIESIS
DSNCLLTMVR SGSKGSNLKV MQQIGSLGFQ VIKGEELLST HKNPKLVRLA ASMGYSMEND
LQDIWEIRGL VKSSLLDGLE PHEFFVHAIS VRDGLFRQSL DIAEPGELFK RLMLFLRDIH
IAYDGTVRNM GGLEIIQFEY DGGKCMTQDS ENKNTLSNKT VMPGDAVGIL AATAISQPAY
QVMLEATQCL ASRKIRPLEL LQESLFPRST SKLKESDRVS ILRLHRCKSD GKYCEERRVL
KLQDELQPVT MEILATETAI AYSSDSSEQW EGLDCAATEL KQTEFFPWVG HVQLDKMVLT
EKKISQEMIL DRLHSKVKIH KSVSRKFRIG NIVFCIRDSC TCDMNIYQET VKLRQKEVVG
PCLHFLLTRS TRGKVRSIKT VKEVSNETVE LLEVLQNFII PEILKTVVKG SEKLQSVNIL
WEDATWSPPV KSEENDSNVM KSGRGELVLE VTVKELYSQS RGMPWRTVQE SCIQFVDYVD
WQRSSPYSIQ EIKSVLGVDA ARDVLLQRLE LAAGNSIGNK HLKLVADFMV YSGEVQGLTS
YGYRDWMRSL KFSSPFTAGA FRAPIKHFLE AGRKGATERF SGVLASSVFG KKVPLGTGAV
FDLNLNMETK FTSSSSTNLN SEGSAESDPG GSVDVLARLI ELNTEIGVQD LSAKSEVDTY
DGNNSCQVIE WGSSPGISKS EGVWDVKNNG PAKTAVDPRN RGDDQNNDAW GTSDNIPQWG
AGVAGRDWPS VETLDPWGQ
//
