ID G7E0H8_MIXOS Unreviewed; 2471 AA.
AC G7E0H8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=Mo03004 {ECO:0000313|EMBL:GAA96338.1};
GN ORFNames=E5Q_03004 {ECO:0000313|EMBL:GAA96338.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA96338.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA96338.1}.
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DR EMBL; BABT02000078; GAA96338.1; -; Genomic_DNA.
DR STRING; 764103.G7E0H8; -.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG4224; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR InParanoid; G7E0H8; -.
DR Proteomes; UP000009131; Unassembled WGS sequence.
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; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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; PF00514; Arm; 5.
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; 11.
DR SMART; SM00185; ARM; 9.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS50176; ARM_REPEAT; 7.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 4.
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:UP000009131};
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 267..571
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REPEAT 1985..2027
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 2026..2068
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 2067..2109
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 2108..2148
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 2151..2193
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 2192..2234
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 2233..2276
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 1578..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2420..2454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2420..2443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2471 AA; 270191 MW; FD8613396AF4F031 CRC64;
MQNAFTYSQA PIRRVRQIQF GILSPEETRA LSVAKIDSPE IYQDVGLGAG SSVGGRPKAG
GLADPRMGTI DRNFKCQTCG EGMAECPGHF GHIELGRPVY HVGFMTKVKK ILECVCVQCG
TLKSDLSELP LADAVRHTQN PKRRLKLVHE VAAKKRQCSR DAPDIQIIKD DDLTGLERRD
EGRASRLAQE YYAGRHGGCG SIQPVIRKEG LKLFLVYDKS TTDDDGGKDK SQEKVPLSAR
RCLEILRSIP ERDLDFMGLS KDEARPEYMI LQILPVPPPP VRPSVSVDGG AMRSEDDLTY
KLIEILRTNQ QLVKLEAEGA GAHILDEFEQ LLQWHIATYM DNDLPGQPQA MQKSGRAVKS
IRARLKGKEG RLRGNLMGKR VDFSARTVIT GDPNLELDEV GVPESIAKNL TYPERVTPYN
ITALQALVAK GPDELPGARY VVKDSGDRID LRYLPSGTSI DLAYGWIVER HLRNGDYVLF
NRQPSLHKMS MMAHRVKLLP YSTFRLNLSV TPPYNADFDG DEMNMHVPQS EETRAELQQI
AWVPRQIVSP QANKPVMGIV QDTLCGIRKF TLRDCFMDRD FVQNIMLWVP EWDGLLPPPA
IVKPKPMWTG KQILSMCIPR GVNLFIDNEA HSSLPDDDSG VLVDDGEIYY GVINKKTVGA
QRESLVDLIF REKGPEICRL FFTGVQKVVN FWLLHNGFSI GIGDTVADRD TMRTITDYIQ
TAKDEVAVFI SKAQQDLIEP EPGMTIRETF ESKVTGSLNR ARDTAGQSAE RSLAASNNVK
QMVVAGSKGS FINISQMSAC VGQQIVEGKR IPFGFRYRSL PHFTKDDHTP EARGFVENSY
LRGLTPQEFF FHAMAGREGL IDTAVKTAET GYIQRRLVKA LEDVMVNYDG TVRNSLGDIV
QFVYGEDGMD GASVERQVIE PIRQSDVGFE RMYRVDITDP AWSFKPGTLQ AGLLEADANL
QDLLDEEYAQ LQEDRALLRQ FIFHNSTAQW PLPVKLFRII QNAQQIFNIN DREPSDLRPA
YIIEAIRDLS EKLVIVRGSD NLTLEAQNNA VLLFRILLRC EMATKRVLHE HHLSREAFDW
VVGEIEARFN ASVVHPGEMC GTLAAQSIGE PATQMTLNTF HYAGVSSKNV TLGVPRLKEI
INIADNIKTP SLTVYLQPGY ARDQQRAKSV SNQLGHVTLR TITASAEIFY DPEPSRTVIE
DDNDFVEAFF AIPDQEVEEN LHRQSPWLLR YELDRAKVLD KGLTMAGIAS KISAVFQSDL
FVIWSEDTAE KLVIRCRTLQ SEEKDDDDDA DEQDEVAFLK RIETHMLDDV ELGGIKGIQR
VYMVDQKKQV ITPAGTWGSE QEWTLETDGL NLRQVLTIDG VDARRTYSNS IVEVYNVLGI
EAARAALLRE LRLVIEFDGS YVNYRHLSLL CDLMTNRGRL MAITRHGINR ADTGALMRCS
FEETVEILME AASVAEKDYC TGVAENVLLG QLAPMGTGAF DTMLDLEALK RVVVDHRLPA
MNMMDEMFMH KTGRTPLQGQ GHSTPYMDVG DGRTPMVDMS FDGLSGAGQF SPVNTGEVML
DGSMTAYGFG SGQTSPYSIG GPGDLNTSPQ GAYSPTSPGY SPASPSYVPT SPNAMGATSP
MFRTSPTSPW VNGALGNTSP AYSPTSPNHY SPASPNFSPA SPRFSPSSPR FSPASPNFSP
ASPNYAPNGQ RRASPTSPQF SPAGHRSPTG QRYSPTSPSY SPTSPAFSPT SPNGLYSPAA
SSRGSRKGSG ASAAASASAR KYSPTSPSYS PTSPAYSPTS PNAMSMASKI SPTSPTSPRG
PQQYSPGSPA MSSPTSPMHS PSSPRFSPSA GADRYAPAGA GRYSPQSGSP AEPHSSGQKR
TAYSASPSWQ QQWLPCTDQC ETCQTSERRR PCNLARKMGV VASCCGCGGG GRGAGYEPLL
LENEREAVAD LLQYLENRAE TNFFTGDPLR SLATLSFSEN VDLQRSAALA FAEITEKDVR
EVSRDTLEPI MFLLQSHDVE VQRAASAALG NLAVNTDNKI LIVKLGGLEP LIRQMLSPNV
EVQCNAVGCI TNLATHDENK TKIAKSGALV PLTRLARSKD MRVQRNATGA LLNMTHSDEN
RQQLVNAGAI PVLVSLLSSP DTDVQYYCTT ALSNIAVDGV NRRKLAQSEP KLVHNLIGLM
DSPSLKVQCQ AALALRNLAS DEKYQIDIVK NRGLDALLRL LNSSFLPLIL SAAACVRNVS
IHPANESPII EAGFLHPLIH LLAYDENEEI ASHAISTLRN LAASSEKNKL AIVEAGAVER
IKELVLNVPL SVQSEMTACA AVLGLSDDIK GQLLDMGICE VLIPLTASPS VEVQGNSAAA
IGNLSSKADD YAAFNAVWTE PEGGLHGYLV RFLDSRDTTF QHIAVWTVVQ LLESGDATLE
HSIKSSSQLM ALIQGLSTSA SAAPSSAGGE PKPSDSVSQT GGSGDEDEEG GEGEIAALAR
RIIDLLDSPQ A
//
