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Database: UniProt
Entry: A0A199UUT7_ANACO
LinkDB: A0A199UUT7_ANACO
Original site: A0A199UUT7_ANACO 
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
//
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