ID A0A094A7I5_9PEZI Unreviewed; 1670 AA.
AC A0A094A7I5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN ORFNames=V493_04710 {ECO:0000313|EMBL:KFY25309.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY25309.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY25309.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:RU363031}.
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:RU363031};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000256|ARBA:ARBA00011730}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU363031}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KFY25309.1}.
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DR EMBL; JPJV01001849; KFY25309.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094A7I5; -.
DR HOGENOM; CLU_000524_5_2_1; -.
DR OrthoDB; 5476750at2759; -.
DR Proteomes; UP000029327; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1070.20; -; 1.
DR Gene3D; 3.90.1100.10; -; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR PANTHER; PTHR20856:SF7; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU363031};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU363031};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029327};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 44..379
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1670 AA; 186359 MW; 28C20AEAEAFD6463 CRC64;
MVSPTDSSSA SRRAQSIAGH LQAPQGRKVT DYKFEGWLGL DKTAAAGNMV WGEFEPKSWT
EDDVDIKVSH CGICGSDIHT LRSGWGPSIY PCCVGHEIIG EAVAVGKNVK NIKVGDRVGV
GAQSGSCLKS SCFECSNGLE NYCTRMVGTY SGKYSDGSKS YGGYSKYVRA PAHFTVQIPK
ELDSAEAAPM LCAGVTMWSP LRKAGAGPGK TVGIVGIGGL GHFGLLWAKA LGCDKVVAIS
RGSSKKEDAL KMGADEFIAT QEDPDWAKKN RRKLDIIIST VSDAKMPLSK YLQLLRTNGR
YIQVGAPEEA IPSFRIGALI AKAVKIEGSS IGSPAELSEM LEFAAKKNIH PFIEKREMKD
ANQAIVDMED GKARYRYVLS ATCGEARRSA EGQPHTRRRA TSTTPLYLVK LRLKMDNLED
QYDEDAYEFE GEAEEPTITA EACWTVISSF FESKGLVSQQ LDSFDEFVST SMQDLINENS
QLTLDQNNPP PVNGEPIQLR RYEIKFRTVF IAEPMMTEGD GTTARLFPQE ARLRNLTYSS
ALYIHLDKKV SIAVERPTPL NELDEDEQAE LAAGGDHPTK VIWEIEDQSM SQEEAAKLPA
NERPVTAEPF FIGKLPIMLK SKYCNLKDMD DEELYGWNEC PYDQGGYFII NGSEKVLIAQ
ERSAANIVQV FKKPPPSPTP FIAEIRSALE KGSRLISSLT IKLHSKGDTQ RGSFGQTIKS
TLPYIKSDIP IAVVFRALGV VSDEDILNHV CYDRKDTQML EMLKPCIEEA FVIQDREVAL
DFIGKRGQSL GVPRDKRIKH ARDIMQKELL PHISQKEGSE TRKAFFLGYM VHKLLQCALG
RRETDDRDHF GKKRLDLAGP LLAKLFRNLF RKLTGDLYKY IQRCVENKKE FNPALGIKAT
TLTNGLKYSL ATGNWGDQKK AASSTAGVSQ VLNRYTFAST LSHLRRTNTP IGRDGKIAKP
RQLHNTHWGL VCPAETPEGQ ACGLVKNLAL MCYVTVGTPS EPIIEFMIQR SMEVLEEYEP
LRSPNATKVF VNGVWVGVHR DPSHLVETVQ DLRRSSLISH EVSLIRDIRD REFKIFTDAG
RVCRPLFVVD NKTDSENNGK LVFNAEHIRR LEDDLALPNN MDLEEKEERG YYGFQGLIND
GVVEYLDAEE EETVMIVMTP QDLEDGRKAR QGYTVAAGPE DSINARVQTK PKATSMVYTH
CEIHPSMILG ICASIIPFPD HNQSPRNTYQ SAMGKQAMGV FLTNFDQRMD TMANILYYPQ
KPLAITRSME YLKFRELPAG QNAIVAILCY SGYNQEDSVI MNQSSIDRGL FRSLFYRAYH
DQEKRIGMNV VEQFEKPFRS DTLKLKHGTY DKLDDDGIVA PGVRISGEDI IIGKTAPLPP
DAEELGQRTK SHTKRDASTP LRSTENGIVD QVLITTNAEG LRFVKVRMRT TKIPQIGDKF
ASRHGQKGTI GITYRQEDMP FTREGIVPDL IINPHAIPSR MTIAHLIECQ LSKVASLIGK
EGDATPFTDV TVDSVSSRLR DMGYQSRGFE IMYHGHTGRK LVAQVFLGPT YYQRLRHMVD
DKIHARARGP TQILTRQPVE GRARDGGLRF GEMERDCMIS HGASAFLKER LFEVSDAFRV
HVCDICGLMT PIAKLNTQSF EFALPGAGVD EYRRQNVHQQ VGSERPVKPR
//
