ID H9GLG5_ANOCA Unreviewed; 1969 AA.
AC H9GLG5;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=POLR2A {ECO:0000313|Ensembl:ENSACAP00000014487.2};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000014487.2, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000014487.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000014487.2};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000014487.2}
RP IDENTIFICATION.
RG Ensembl;
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_003228555.1; XM_003228507.3.
DR STRING; 28377.ENSACAP00000014487; -.
DR Ensembl; ENSACAT00000014782.4; ENSACAP00000014487.2; ENSACAG00000014561.4.
DR GeneID; 100561860; -.
DR KEGG; acs:100561860; -.
DR CTD; 5430; -.
DR eggNOG; KOG0260; Eukaryota.
DR GeneTree; ENSGT00930000151033; -.
DR HOGENOM; CLU_000487_0_1_1; -.
DR InParanoid; H9GLG5; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR TreeFam; TF103036; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000014561; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
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; 25.
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; 21.
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};
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:UP000001646};
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 245..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1545..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1969 AA; 217090 MW; 28274B32B293C6A7 CRC64;
MHGGAPSGDS ACPLRTIKRV QFGILSPDEM KRMSVTEGGI KYPETTEGGR PKLGGLMDPR
QGVIERTGRC QTCAGNMTEC PGHFGHIELA KPVFHVGFLG KTMKVLRCVC FFCSKLLVDS
NNPKIKDILA KSKGQPKKRL THVYDLCKGK NICEGGEEMD NKFGVEQPEG DEDITKEKGH
GGCGRYQPRI RRSGLELYAE WKHVNEDSQE KKILLSPERV HEIFKRISDE ECFILGMDPK
FARPEWMICT VLPVPPLSVR PAVVMQGSAR NQDDLTHKLA DIVKINNQLR RNEQNGAAAH
VIAEDVKLLQ FHVATMVDNE LPGLPRAMQK SGRPLKSLKQ RLKGKEGRVR GNLMGKRVDF
SARTVITPDP NLSIDQVGVP RSIAANMTFA EIVTPFNIDR LQELVRRGNS QYPGAKYIIR
DNGDRIDLRF HPKPSDLHLQ IGYKVERHMC DGDIVIFNRQ PTLHKMSMMG HRVRILPWST
FRLNLSVTTP YNADFDGDEM NLHLPQSLET RAEIQELAMV PRMIVTPQSN RPVMGIVQDT
LTAVRKFTKR DVFLERGEVM NLLMFLSTWD GKVPQPAILK PRPLWTGKQI FSLIIPGHIN
CIRTHSTHPD DEDSGPYKHI SPGDTKVIVE NGELIMGILC KKSLGTSAGS LVHISYLEMG
HDVTRLFYSN IQTVINNWLL IEGHTIGIGD SIADAKTYQD IQNTIKKAKQ DVIEVIEKAH
NNELEPTPGN TLRQTFENQV NRILNDARDK TGSSAQKSLS EYNNFKSMVV SGAKGSKINI
SQVIAVVGQQ NVEGKRIPFG FKHRTLPHFI KDDYGPESRG FVENSYLAGL TPTEFFFHAM
GGREGLIDTA VKTAETGYIQ RRLIKSMESV MVKYDATVRN SINQVVQLRY GEDGLAGESV
EFQNLATLKP SNKAFEKKFK FDYTNERALR RTLQEEMVKD ILSNAHIQNE LEREFEKMKE
DREVLRVIFP TGDSKVVLPC NLLRMIWNAQ KIFHINTRLP SDLHPIKVVD GVKELSKKLV
IVNGDDPLSK QAQENATLLF NIHLRSTLCS RRMIEEFRLS GEAFDWLLGE IESKFNQAIA
HPGEMVGALA AQSLGEPATQ MTLNTFHYAG VSAKNVTLGV PRLKELINIS KKPKTPSLTV
FLLGQSARDA ERAKDILCRL EHTTLRKVTA NTAIYYDPNP QNTVVAEDQE WVNVYYEMPD
FDVTRISPWL LRVELDRKHM TDRKLTMEQI AEKINAGFGD DLNCIFNDDN AEKLVLRIRI
MNSDENKMQE EEEVVDKMDD DVFLRCIESN MLTDMTLQGI EQISKVYMHL PQTDNKKKII
ITEDGEFKAL QEWILETDGV SLMRVLSEKD VDPVRTTSND IVEIFTVLGI EAVRKALERE
LYHVISFDGS YVNYRHLALL CDTMTCRGHL MAITRHGVNR QDTGPLMKCS FEETVDVLME
AAAHGESDPM KGVSENIMLG QLAPAGTGCF DLLLDAEKCK YGMEIPTNIP GLGVGGPTGM
FFGSAPSPMG GMSPAMTPWN QGATPAYGAW SPSVGSGMTP GAAGFSPSAA SDASGLSPGY
SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP SYSPTSPAYE PRSPGGYTPQ SPSYSPTSPS
YSPTSPSYSP TSPNYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT
SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY
SPTSPNYSPT SPNYTPTSPS YSPTSPSYSP TSPNYTPTSP NYSPTSPSYS PTSPSYSPTS
PSYSPSSPRY TPQSPTYTPS SPSYSPSSPS YSPTSPKYTP TSPSYSPSSP EYTPTSPKYS
PTSPKYSPTS PKYSPTSPTY SPTTPKYSPT SPTYSPTSPV YTPTSPKYSP TSPTYSPTSP
KYSPTSPTYS PTSPKGSTYS PTSPGYSPTS PTYSLTSPAI SPDDSDEEN
//
