ID F1KQ31_ASCSU Unreviewed; 1867 AA.
AC F1KQ31;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY39985.1};
RN [1] {ECO:0000313|EMBL:ADY39985.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
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; JI164047; ADY39985.1; -; mRNA.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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; 28.
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; 10.
PE 2: Evidence at transcript level;
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 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 238..541
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1610..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 934..961
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1867 AA; 204825 MW; D675597F4693FD10 CRC64;
MALVGLDFRA PLRTVKRVQF GILSPDEIKR MSVGEIEFSE IYENGKPKMG GLMDPRQGVV
DRRGRCMTCA GNLADCPGHF AHLELAKPVF HIGFITKTLK ILRCVCFYCS RLLIDKDAPR
VKEILKKTVG NPRRRLALIY DLCKSKSVCE GGDELQNVGG EEGEEGEKEV KAGGCGRYQP
SYRRTGIEIN AEWKRHVNED TQERKIVLTA ERALEIFKGI SDADCLVIGM DPRFARPDWM
IAQVLPVPPL AVRPAVVTFG SARNQDDLTH KLSDIVKTNN QLRRNEANGA AAHVIAEDVK
LLQYHVATLV DNCIPGLPTA TQKGGRPLKS IKQRLKGKEG RIRGNLMGKR VDFSARTVIT
PDPNLPIDTV GVPRTIAQNM TFPEIVTPFN VDKLQELVNR GDSQYPGAKY IIRDNGARVD
LRYHPRAADL LLQPGYRVER HMKDGDIIVF NRQPTLHKMS MMGHRVKILP WSTFRMNLSV
TTPYNADFDG DEMNLHLPQS LETKAEISEI AMVPRQLITP QANKPVMGIV QDTLTAVRMM
TKRDVFIELP RMMDLLMQMP NWDGKIPQPA ILKPKPLWTG KQVFTLIIPG NVNVLRTHST
HPDDEDSGPY KWISPGDTKV IIEHGELLAG IICSKTIGRS AGNLLHVVTL ELGWEVAAHF
YSHIQTTVNA WLLAEGHTIG IGDTIADQAT YKDIQETIRK AKYDVVEVIE KAHNDELEPT
PGNTLRQTFE NMVNRILNDA RDRTGGSAQR SLSEFNNFKA MVVAGSKGSK INISQVIACV
GQQNVEGKRI PFGFRHRTLP HFIKDDYGPE SKGFVENSYL AGLTPSEFFF HAMGGREGLI
DTAVKTAETG YIQRRLIKAM ESVMVNYDGT VRNSIAQMVQ LRYGEDGLDG MWVENQSMPS
MKPTNALFEK EFKLDLSDEK SLRKMYTENV IRDLQGSAEA LKEVESEWAQ LEEDRRLLRK
IFPKGDAKIV LPCNLQRLIW NAQKIFRVET RKPTDLNPLH VIDGVRELSK KLVIVSGDDR
ISKQAQYNAT LLMNILLRST LCSKRMAEKH KLNMEAFEWL IGEIESRFKQ AIVQPGEMVG
AIAAQSLGEP ATQMTLNTFH YAGVSAKNVT LGVPRLKEII NVSKKPKTPS LTVFLTGTAA
KDAEKAKDVL CKLEHTTLRK VTANTAIYYD PDPKNTVIEE DEEWVNIFYE MPDFDPSRAS
PWLLRIELDR KRMTDKKLTM EAIADKIHHG FGDDLNVIYT DDNAEKLVFR LRITNQDGDK
GNEEEQVDKM EDDVFLRCIE SNMLSDLTLQ GIESITKVYM HKPTTDDKKR VVITPDGGFK
AIPEWLLETD GTALAKVLSE QNVDSVRTTS NDICEIFEVL GIEAVRKAIE REMNHVISFD
GSYVNYRHLA LLCDVMTAKG HLMAITRHGI NRQEVGALMR CSFEETVDIL MEAAAHAEQD
PVKGVSENIM LGQLARAGTG CFDLVLDADK CKLGMEIQAG SGLLGGGGMY FAGGASPASS
SMSPAQTPWN AATTPAYGAA WSPAVGSGMT PGVAGFSPSG HSEGGFSPYG GGAWSPASPG
GSLGAMSPSG AYSPASDYGS GLDALKSPSY SPTSPASAYG ASSPAYGVMS PRYSPTSPSY
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPAS
PGYSPSSPRY SPTSPTYSPT SPTYSPTSPT YSPTSPTYSP TSPSYSPASP GYSPTSPRYS
PTSPTYSPTS PAYSPSSPQY SPSSPQYSPS SPQYTPSSPM GGDASPAYSP SSPQYSPSSP
RYSPSSPQYS PSSPQYSPSS PGGAGTTYSP SSPQYSPSSP QYSPSSPQYS PSSPQYSPSS
PQYSPGD
//
