ID A0A1R3JZ87_COCAP Unreviewed; 1928 AA.
AC A0A1R3JZ87;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=CCACVL1_03458 {ECO:0000313|EMBL:OMP00131.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMP00131.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMP00131.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMP00131.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) 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:OMP00131.1}.
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; AWWV01006701; OMP00131.1; -; Genomic_DNA.
DR STRING; 210143.A0A1R3JZ87; -.
DR EnsemblPlants; OMP00131; OMP00131; CCACVL1_03458.
DR Gramene; OMP00131; OMP00131; CCACVL1_03458.
DR OMA; WGSQQKS; -.
DR OrthoDB; 455034at2759; -.
DR Proteomes; UP000188268; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02737; RNAP_IV_NRPD1_C; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.450.40; -; 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; 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; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF51; DNA-DIRECTED RNA POLYMERASE V SUBUNIT 1; 1.
DR Pfam; PF11523; DUF3223; 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; 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
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 205..504
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1366..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..1919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1928 AA; 213837 MW; 458DBB878D0A6BC0 CRC64;
MEENSSAIIL DSEIVGLRFC LASPKEISTA SFNGFPITHI SPLSNSYLGL PLECGGSCGA
CGTNEPGKCE GHFGYIELPV PIYHPSHIDE LKRLLSLLCL KCLKLKNKFQ IKSGSVAERL
LASCCENSPH VSIDVKRKGG SACYLELKQP SRQGPTSWKF LERYGFRYGD HPKRTLLPCE
VVNILKKIPA ETRRKLSGKG FFPQEGYILH YLPVPPNCLS VPDISDGVSV MSSDLSTSML
KKVLKQTEII SKSRSGTPNF ESHEVEANDL QYAVEEYLQV RGTVKASRNI DARYGVSKDS
SGSSTKAWLE KMRTLFIRKG SGFSSRSVIT GDPYKRVNEI GIPSEIAQRI TFEERVNSHN
MTYLQNLVDN KMCLTYRDGS SAYSLREGSK GHTFLRPGQV VHRRIMDGDI VFINRPPTTH
KHSLQALSVY VHDDHTVKIN PLICGPLSAD FDGDCIHLFY PQSLAAKAEV LELFSVEKQL
LSSHNGNLNL QLATDSLLSL RVMLKTFLFK KADVQQLSMY LSSALPQPAL LKGNSFGPCW
TAFQILQTAF PACLDCSSNR YLIGKSEILK VDFGRELMPS VINEVVTSIF FEKGPKEVLE
FFDSLQPLLM ENIFAEGFSL SLEDFSISRE AIEDIEKDVQ LISPLLYQLR STYNELVGLQ
IENHIREAKV PVANFIRKSS AFGDLIDSKS DSAVTKVVQQ IGFLGQQLFD KGKFYSKTLV
DDVAYQFQSI YPSDLVDYPS AEFGLIKSCF FRGLDPYEEM VHSISTREVI VRSSRGLSEP
GTLFKNLMAI LRDVVICYDG TVRNVNSNSI IQFQYGLNAR TKPQFPAGEP VGVLAATAMS
NPAYKAVLDS TPSSNSSWEL MKEILQCKVS FKNELIDRRV ILYLKDCNCG RKYCQENAAY
VVKNHLRKVT LKDAAKELVI EYKQQQAEPE SEAGLVGHIL LNKELLKELN VSMQEIHMKC
QETITSSRKN KLTADTFKRA DLFFNECCSI QQSCGGKWLD MPCLMFVCRN SQDLDSSLQD
LSDIIYPALL ETVIKGDPRI CSANIIWVSP DTTTWIRNPS KSQKGELALD VVLEKSAVKQ
NGDAWRTVMD CCLPVLNLID TQRSIPYAIK QVQDLLGISC AFEQAVQRLS TSVSMVAKGV
LREHLILLAN SMTCAGNLIG FNSGGYKALC RSLNIQVPFT EATLFTPRKC FERAAEKCHV
DSLSSIVASC SWGKHVAVGT GSRFDVLWDH KEVGFDQRSG IDVYNFLGML SGVKGPTSNT
ACLGEEVDDL MELDDMGEWS ISPDHGAGSD KPVFEDAANF ENDLEDQPAE STWDKVASST
ENVGWDAFSA WNKNAEDGDK FAEAGAGTTK QTEWSNWGTS KSKTQDFVED QTDSSGWGMN
KSDTGVLPVK EKTSKSNGWD AGTSWATSTP KQNEWCDWRT NKSKTQDVVS PKVDRLSMKE
PAELSGWGKE KPDAEDGKTF KSNGWDAGTS FESSKSGGWN QQKSVEDSQV WGSQHNSADH
SPGWGSQQKS ANRSQGWDSQ KKSEDPLPGW GSQKKSVDRS QDWDSHQKSP KQTQGWGSQK
KSMDHSQGGG LQEKSPEPSQ GWGSQQKSPE PSQGWGSQQK SPEPSQGWGS QQKSAEPSQG
WGSQQKSAEP SQGRGSQQKS PEPSQGWGSQ QKSAEPSQGW GSQQKSPEPS QGWGSQQKSP
EPSQGWGSQQ KSAWGSLDES NRQASTNGWG RQGGEDATEG EQQHQWGGKT KGSRRWASDA
GKKKPSVKSV NDDSSMAAMY TATRQRLDMF TSEEQDILSE IEPLMQSCRK IFRQPGYNDG
DPLPASDQSF VLDNIFTHHP DKAAKMGAGV DYVMISKHTD FQDTRCFYVV STDGQKEDFS
YRKCLESFVK GKYPEMADAF IEKYFKKTRP GGNRERSASV APDEGENQHP HRERSVSVAP
EEGENNGQ
//
