ID I7A065_9ASCO Unreviewed; 872 AA.
AC I7A065;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 Aciculoconidium aculeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Aciculoconidium.
OX NCBI_TaxID=43968 {ECO:0000313|EMBL:AFO11428.1};
RN [1] {ECO:0000313|EMBL:AFO11428.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL YB-4298 {ECO:0000313|EMBL:AFO11428.1};
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}.
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DR EMBL; JQ713039; AFO11428.1; -; Genomic_DNA.
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:AFO11428.1"
FT NON_TER 872
FT /evidence="ECO:0000313|EMBL:AFO11428.1"
SQ SEQUENCE 872 AA; 98128 MW; 950A7CC73815E487 CRC64;
NKNFEENEQP ERRLLTPSEI LNVLKHIXPE DCHKLGFNED YARPEWMLIT VLPVPPPPVR
PSIAFNDTAR GEDDLTFKLA DVLKANINVQ KLEMDGSPQH VISEFEALLQ FHVATYMDND
IAGQPQALQK TGRPIKSIRA RLKGKEGRLR GNLMGKRVDF SARTVISGDP NLDLDQVGVP
ISIARTLSYP EIVTPYNIHR LTEFVRNGPN EHPGAKYVIR DTGDRIDLRY NKRAGDIALQ
YGWKVERHLM DDDPVLFNRQ PSLHKMSMMA HRVKVMPYST FRLNLSVTSP YNADFDGDEM
NLHVPQSPET RSELSQICAV PLQIVSPQSN KPVMGIVQDT LCGVRKMTLR DIYIEYDQVM
NICYWIPNWD GVIPPPAIVK PKPLWTGKQL LSMAIPKGIH LQRFDGGKDM LSPNDTGMLI
VDGEIMFGVV DKKTVGATGG GLIHTVMREK GPQVCAKLFS SIQKVVNYWL LHNGFSIGIG
DTIADAGTXK TITSTIQEAK EKVXEIILDA QQNRXEPEPG MTLRESFEHN VSRILNQARD
TAGRSAEMNL KDLNNVKQMV TSGSKGSFIN ISQMSAXVGQ QIVEGKRIPF GFSDRTLPHF
TKDDYSPESK GFVENSYLRG LTPQEFFFHA MAGREGLIDT AVKTAETGYI QRRLVKALED
IMVHYDGTTR NSLGDIVQFV YGEDGIDGTQ VEKQSVDTIP GSDASFEKRY RIDVLDPSKS
IPEASLESGK EIKGDVKVQK VLDEEYNQLL DDRQYLREVC FPNGDSSWPL PVNLRRIVQN
AQQIFHNGRH KASDLRLEEI VHGVQQLCTK LLVIRGSTAL MKEAQENATL LFQCLLRSRL
AARRVIEEFK LNRASFEWVV GEVEAQFQKS IV
//