ID A0A199UUT7_ANACO Unreviewed; 1854 AA.
AC A0A199UUT7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=LOC109727514 {ECO:0000313|RefSeq:XP_020113244.1};
GN ORFNames=ACMD2_13652 {ECO:0000313|EMBL:OAY68410.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY68410.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY68410.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY68410.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
RN [2] {ECO:0000313|RefSeq:XP_020113244.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_020113244.1};
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 EMBL; LSRQ01004943; OAY68410.1; -; Genomic_DNA.
DR RefSeq; XP_020113244.1; XM_020257655.1.
DR STRING; 4615.A0A199UUT7; -.
DR EnsemblPlants; Aco009331.1.mrna1; Aco009331.1.mrna1; Aco009331.1.path1.
DR GeneID; 109727514; -.
DR Gramene; Aco009331.1.mrna1; Aco009331.1.mrna1; Aco009331.1.path1.
DR OrthoDB; 7998at2759; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR Proteomes; UP000515123; Linkage group 22.
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 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; 16.
DR PRINTS; PR01217; PRICHEXTENSN.
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; 13.
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};
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:UP000092600};
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 243..549
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 695..722
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1541..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1854 AA; 206487 MW; 2A9AE3FB15747775 CRC64;
MDMRFPFSPA EVAKVRTVQF GILSPDEIRQ MSVVQIEHSE TMERGKPKPG GLSDPRLGTI
DRKMKCETCM ANMAECPGHF GHLELAKPMF HIGFLKTVLA IMRCVCFNCS KILADEDDTR
FKQALKIRNP KNRLKRIYDA CKSKKRCAGG DDIDVQGQQD TDEPVKKSRG GCGAQQPNIT
VDGMKMVAEF KASKKKSDDQ EQLPEPVERK QILSAERVLN VLKRISDEDC LLLGLNPKYA
RPDWMILQVL PIPPPPVRPS VMMDTSSRSE DDLTHQLAMI IRHNENLRRQ ERNGAPAHII
TEFAQLLQFH IATYFDNELP GQPRATQRSG RPIKSICSRL KAKEGRIRGN LMGKRVDFSA
RTVITPDPTI NIDELGVPWS IALNLTYPET VTPYNIERLK ELVEYGPHPP PGKTGAKYII
REDGQRLDLR YLKKSSDQHL ELGYKVERHL QDGDYVLFNR QPSLHKMSIM GHRIKIMPYS
TFRLNLSVTS PYNADFDGDE MNMHVPQSFE TRAEVLELMM VPKCIVSPQS NRPVMGIVQD
TLLGCRKITK RDTFIEKDVF MNILMWWEDF DGKIPAPAIL KPRPLWTGKQ VFNLIIPKQI
NLIRTSAWHL ESETGFITPG DTLVRIEKGE LLSGTLCKKT LGTSTGSLIH VIWEEVGPDA
ARKFLGHTQW LVNYWLLQNG FSIGIGDTIA DAATMEKINE TISKAKNEVK ELIKLAQEKQ
LEAEPGRTMM ESFENRVNQV LNKARDDAGS SAQKSLSESN NLKAMVTAGS KGSFINISQM
TACVGQQNVE GKRIPFGFIG RTLPHFTKDD YGPESRGFVE NSYLRGLTPQ EFFFHAMGGR
EGLIDTAVKT SETGYIQRRL VKAMEDIMVK YDGTVRNSLG DVIQFLYGED GMDAVWIESQ
KLDSLKMKKS EFDNVFTYEI DDPNWNPSYM LPEHVDDLKS IKEFRNVFEA EVQKLEADRI
QLGTEIATTG DNTWPMPVNL KRLIWNAQKT FKIDLRRPSD MHPMEIVEAI DKLQERLKVV
PGDDLMSIEA QKNATLFFNI LLRSTFASKR VLKEYRLTRE AFEWVIGEIE SRFLQSLVAP
GEMIGCVAAQ SIGEPATQMT LNTFHYAGVS AKNVTLGVPR LREIINVAKK IKTPSLSVYL
KPEINKKKEM AKNVQCALEY TTLRSVTHAT EIWYDPDPLG TLIEEDVEFV KSYYEMPDED
IAPEKISPWL LRIELNREMM VDKKLSMADI AEKINHEFDD DLTCIFNDDN ADKLILRIRI
MNDEAPKGEL QDESAEDDVF LKKIESNMLT EMALRGIPDI HKVFIKSGKV NRFDKSEGFK
PDVEWMLDTE GVNLLAVMCH EDVDATRTTS NHLIEVIEVL GIEAVRRALL DELRVVISFD
GSYVNYRHLA ILCDTMTYRG HLMAITRHGI NRNDTGPLMR CSFEETVDIL LDAAVYAESD
HLRGVTENIM LGQLAPIGTG GCSLYLNDQM LQQAIELQLP SYIEGLEFGM TPARSPISGT
PYHESMMSPS YFMSPNVRSS PITDAQFSPY VGGMVFSPGS SPGYSPSSPG YSPSSPGYSP
TSPGYSPTSP GYSPTSPGYS PTSPTYSPSS PGYSPTSPAY SPTSPSYSPT SPSYSPTSPS
YSPTSPSYSP TSPTYSPTSP SYSPTSPAYS PTSPAYSPTS PAYSPTSPSY SPTSPSYSPT
SPSYSPTSPS YSPTSPSYSP TSPTYSPTSP SYSPTSPAYS PTSPGYSPTS PSYSPTSPTY
SPTSPSFNPP SAKYSPSHAY SPSSPRLSPY SQTSPNYSPT SPSYSPTSPS FTPPSPTYSP
TSPYNPGGNP DYSPTSPQYS PSASYSPTAP GYSPSSTSQY SPQMSNKDDE STHG
//