ID A0A1U8IDR2_GOSHI Unreviewed; 1863 AA.
AC A0A1U8IDR2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=LOC107895585 {ECO:0000313|RefSeq:XP_016676336.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016676336.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016676336.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016676336.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_016676336.1; XM_016820847.1.
DR STRING; 3635.A0A1U8IDR2; -.
DR PaxDb; 3635-A0A1U8IDR2; -.
DR Proteomes; UP000189702; Chromosome 2.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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 CDD; cd02733; RNAP_II_RPB1_N; 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; 2.
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; 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 Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 18.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 15.
PE 3: Inferred from homology;
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:UP000189702};
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 242..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1863 AA; 207398 MW; 8688A8FF5DE32AE9 CRC64;
MDLRFAFSPA EVAKVRVVQF GILSPDEIRQ MSVVQIEHSE TTERGKPKVG GLSDPRLGTI
DRKLKCETCT ANMAECPGHF GHLELAKPMF HIGFMKTVLS IMRCVCFNCS KILADEEDHK
FKQALKIKNP KNRLKKILDA CKNKTKCEGG DEIDVQGQDT EEPVKKSRGG CGAQQPKLSI
DGMKMIAEYK AQRKKNDDPE QLPEPVERKQ TLTAERVLSV LKRISDEDCQ LLGLNPKYAR
PDWMILQVLP IPPPPVRPSV MMDTSSRSED DLTHALAMII RHNENLRRQE RNGSPAHIIS
EFAQLLQFHV ATYFDNELPG LPRATQRSGR PIKSICSRLK AKEGRIRGNL MGKRVDFSAR
TVITPDPNIN IDELGVPWSI ALNLTYPETV TPYNIERLKE LVEYGPHPPP GKTGAKYIIR
DDGQRLDLRY LKKSSDHHLE LGYKVERHLN DGDFVLFNRQ PSLHKMSIMG HRIRIMPYST
FRLNLSVTSP YNADFDGDEM NMHVPQSFET RAEVLELMMV PKCIVSPQSN RPVMGIVQDT
LLGCRKITKR DTFIEKDVFM NILMWWEDFD GKVPAPAILK PRPLWTGKQV FNLIIPKQIN
LLRTSAWHSE SETGSITPGD TQVRIEKGEV LSGTLCKKTL GTSSGSLIHV IWEEVGPDAA
RKFLGHTQWL VNYWLLQNAF SIGIGDTIAD AATMEKINET ISKAKDDVKQ LIVKAQNKDL
EPEPGRTMME SFENKVNQVL NKARDDAGNS AQKSLSESNN LKAMVTAGSK GSFINISQMT
ACVGQQNVEG KRIPFGFIDR TLPHFTKDDY GPESRGFVEN SYLRGLTPQE FFFHAMGGRE
GLIDTAVKTS ETGYIQRRLV KAMEDIMVKY DGTVRNSLGD VIQFLYGEDG MDAVWIESQK
LDSLKMKKSE FDRFFRYKID DENWNPTSYM LPEHIEDLRT IQELRDVFDA EVNKLEADRY
QLGTEIAVTG DSNWPLPVNL KRLIWNAQKT FKVDFRRVSD LHPVEIVDSV DKLQERLKVV
PGADPLSVEA QKNATLFFCI LLRSTLASKR VLQEYRLTKE AFEWVIGEIE SRFLQSLVAP
GEMIGCVAAQ SIGEPATQMT LNTFHYAGVS AKNVTLGVPR LREIINVAKK IKTPSLSVYL
SPEASKTKEK AKNVQCALEY TTLRSVTHAT EVWYDPDPMS TIIEEDIDFV KSYYEMPDEE
VAPEKISPWL LRIELNREMM VDKKLSMADI AEKINLEFDD DLTCIFNDDN AEKLILRIRI
MNDEAPKGEL NDESAEDDVF LKKIESNMLT EMALRGIPDI NKVFIKHSKA SKFDEADGYK
TGEEWMLDTE GVNLLAVMCH EDVDARRTTS NHLIEVIEVL GIEAVRRSLL DELRVVISFD
GSYVNYRHLA ILCDTMTYRG HLMAITRHGI NRNDTGPMMR CSFEETVDIL LDAAVYAESD
YLRGVTENIM LGQLAPIGTG DCALYLNDEM LKNAIELQLP SYMEGLEFGM TPARSPVSGT
PYHEGMMSPS YLLSPNLRLS PISDAQFSPY VGGMAFSPTS SPGYSPSSPG YSPSSPGYSP
TSPGYSPTSP GYSPTSPGYS PTSPTYSPSS PGYSPTSPAY SPTSPSYSPT SPSYSPTSPS
YSPTSPSYSP TSPSYSPRSP SYSPTSPSYS PTSPVYSPTS PAYSPTSPAY SPTSPSYSPT
SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP AYSPTSPGYS PTSPSYSPTS PSYSPTSPSY
NPQSAKYSPS LAYSPSSPRL SPSSPYSPTS PNYSPTSPSY SPTSPSYSPS SPTYSPSRLF
FVLFSETSPY NSGVSPDYSP SSPQYSPSAG YSPSAPGYSP TSTSQYTPSN KDGRSNKDDR
SKR
//
