ID I7A0A2_9ASCO Unreviewed; 865 AA.
AC I7A0A2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Flags: Fragment;
OS Yamadazyma philogaea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=45510 {ECO:0000313|EMBL:AFO11448.1};
RN [1] {ECO:0000313|EMBL:AFO11448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL Y-7813 {ECO:0000313|EMBL:AFO11448.1};
RX PubMed=22978764; DOI=10.1111/1567-1364.12006;
RA Kurtzman C.P., Robnett C.J.;
RT "Relationships among genera of the Saccharomycotina (Ascomycota) from
RT multigene phylogenetic analysis of type species.";
RL FEMS Yeast Res. 13:23-33(2013).
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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ713059; AFO11448.1; -; Genomic_DNA.
DR AlphaFoldDB; I7A0A2; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 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; 1.
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; 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; 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 SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 45..348
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO11448.1"
FT NON_TER 865
FT /evidence="ECO:0000313|EMBL:AFO11448.1"
SQ SEQUENCE 865 AA; 97397 MW; 02AED8FE2BD33806 CRC64;
GKGAESDDQP ERRLLTPSEI LNVFRHISSY DCFKLGFNED YARPEWMLIT VLPVPPPPVR
PSIAFNDTAR GEDDLTFKLA DVLKANINVQ RLEMDGSPQH VISEFEALLQ FHVATYMDND
IAGQPQALQK TGRPIKSIRA RLKGKEGRLR GNLMGKRVDF SARTVISGDP NLDLDQVGVP
LSIARTLSYP EIVTPFNIHR LTEYVRNGPN EHPGAKYVIR DSGDRIDLRY NKRAGDIALQ
YGWKVERHLM DDDPVLFNRQ PSLHKMSMMA HRVKVMPYST FRLNLSVTSP YNADFDGDEM
NLHVPQSQET RAELSQICAV PLQIVSPQSN KPVMGIVQDT LCGIRKMTLR DNFIELDQVM
NMLYWIPTWD GVIPPPAVMK PKPLWTGKQL LSIAIPKGIH LQRLESSLLS PKDNGMLIVD
GEIMFGVVDK KTVGSTGGGL IHTVFREKSP QVCAQLFSNI QKVVNFWLLH NGFSIGIGDT
IADSETMKVV TTTIEEAKSK VQDIIMNAQR DKLEPEAGMT LRETFENNVS RVLNQARDTA
GRSAEMSLKD LNNVKQMVTS GSKGSFINIS QMSACVGQQI VEGKRIPFGF ADRTLPHFTK
DDYSPESKGF VENSYLRGLT PQEFFFHAMA GREGLIDTAV KTAETGYIQR RLVKALEDIM
VHYDGTTRNS LGDIVQFLYG EDGMDGTQVE KQSVDTIPGS DAVFEKRYKI DLLHDELPIE
SAKEIKGDVE LQKVLDEEFE QLKKDREYLR TVCFPNGDSS WPLPVNMRRI VQNAQQIFHS
GRQKVSDLKL DEVVNDVKDL CSKLLVVRGD SPLAKEAQEN ATLLFQCLVR SRLAARRVIE
EYKLNKVSFE WVVGEIENQF QKSAV
//
