ID A1YIC5_9FUNG Unreviewed; 960 AA.
AC A1YIC5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
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;
GN Name=RPB1 {ECO:0000313|EMBL:ABM27004.1};
OS Chytriomyces hyalinus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Chytriomyces.
OX NCBI_TaxID=4814 {ECO:0000313|EMBL:ABM27004.1};
RN [1] {ECO:0000313|EMBL:ABM27004.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JEL345 {ECO:0000313|EMBL:ABM27004.1};
RX PubMed=17010206; DOI=10.1186/1471-2148-6-74;
RA Liu Y.J., Hodson M.C., Hall B.D.;
RT "Loss of the flagellum happened only once in the fungal lineage:
RT phylogenetic structure of kingdom Fungi inferred from RNA polymerase II
RT subunit genes.";
RL BMC Evol. Biol. 6:74-74(2006).
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; EF014391; ABM27004.1; -; Genomic_DNA.
DR AlphaFoldDB; A1YIC5; -.
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; 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; 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 128..426
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABM27004.1"
FT NON_TER 960
FT /evidence="ECO:0000313|EMBL:ABM27004.1"
SQ SEQUENCE 960 AA; 107800 MW; FFC856095EDD80BB CRC64;
HILLNCPMYN IGYIKTVKKI LECVCHRCAR LRLQPGDHKY RKLTMIKDKF KYAWESCKNK
VVCEYPDCET QLLPIRRHGI ELFFDQKKVD NKLPRVPLYA DQAKSILEKI TDETCRLLGL
NPDSSRPEWM IFTVIPVPPP CMRPSVHIDV ANGGKGEDDL THMLTNIIRY NNLLGKNESS
KTAIEYKEQL QIHITTYIDN EVSGVPPALQ KGGRMIKSLS ARLKGKEGRI RGHLMGKRVD
FSARTVITGD PHISIEEVGV PLSVAKTLTF PERVTSYNLD RMQALVNNAK NYPGARYVIN
ERGRRIDLEV AKTTPLIEIG DIVERHMVTG DTVLFNRQPS LHKMSMMAHI VRVMPYSSFR
LNVNVCAPYN ADFDGDEMNL HMPQSYETVA ELQTLSMVSS LLVSPQSNKP VNGLVQDALC
GIRKLTMRDT FVNFEDMMDL VMCLKEFPVI PPPAIFKPIP LWTGKQIISL CLPDIDLTGN
TLTHADHEDI FRSTTKDLNE TCTRKAESEF YSATPTDSRV LIQSGIIVHG YLCKKTVGAS
SGGIVHIIYN DHGPRAACDF IDNSSRIVNA WLTNSGFSVG IGDALVSEIT HAVFSSTIDT
QLHKVQKTIE SYHANELKPE GNFDCEQTKE NQIVGLLAKA RDSAGKTTLI SGHPDNNLKQ
MVEAGSKGSV LNICQVSACV GQQMVEGKRI PFGFKDRTLP HFTKYDHSPA ARGFVRNSFV
KGLTPSELFF HAMGGREGLI DTAIKTAETG YIQRRLVKAL EDITVKSDGT VRNSRDDIIQ
FYYGEDGFDG TAIEYQTFPT MMLSESELYS RYYNGIDSEY AQLKKDQELL RRVLRLAEDR
WPLPLNIMRM IITVKKRAIT RGLPDTEFTA EYIFQQTKAV VNSLRPSKLN INSEYNVSAL
FGILVSSILS SKQVLYVHKL SKCQFDYLLI LIKEKYHRGL VQAGESVGVI AAQSIGEPAT
//
