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Database: UniProt
Entry: I7A065_9ASCO
LinkDB: I7A065_9ASCO
Original site: I7A065_9ASCO 
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
//
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