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Entry: A0A1B9HZN4_9TREE
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ID   A0A1B9HZN4_9TREE        Unreviewed;      1439 AA.
AC   A0A1B9HZN4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=I206_05478 {ECO:0000313|EMBL:OCF48698.1};
OS   Kwoniella pini CBS 10737.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF48698.1, ECO:0000313|Proteomes:UP000094020};
RN   [1] {ECO:0000313|EMBL:OCF48698.1, ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF48698.1,
RC   ECO:0000313|Proteomes:UP000094020};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) 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: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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; KI894013; OCF48698.1; -; Genomic_DNA.
DR   RefSeq; XP_019009917.1; XM_019157199.1.
DR   STRING; 1296096.A0A1B9HZN4; -.
DR   GeneID; 30173847; -.
DR   OrthoDB; 169836at2759; -.
DR   Proteomes; UP000094020; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd02736; RNAP_III_Rpc1_C; 1.
DR   CDD; cd02583; RNAP_III_RPC1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR035698; RNAP_III_Rpc1_C.
DR   InterPro; IPR035697; RNAP_III_RPC1_N.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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   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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094020};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          256..565
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1439 AA;  159946 MW;  8D5067D42747E9BF CRC64;
     MDPWAPIDQN EKRYVSSDVP RRIKHIQFQP FTPKDIVRIS EVQVSHSDLY QNHEDGSRTT
     ASHGPLDGRM GPNEKGKKCL TCGEEAAKCV GHYGYVKLAL PVFHIGYFRP TINMLSCICK
     TCARVLLPTN ERTTYLKRFR RPGLESLQRQ SASKAVLASC KKRNICGYCG AANGVVKKSG
     PMKISHEPYR ATKMAALKDE WMSTFKTAVA DNSAVATHLS KAVEDLNPLK VLDLFKRVTA
     EDCELLSLHP DIGRPEDYIW QYISVPPPCI RPSVASEAGN NEDDLTAKLA EIVNINNNVS
     IMMDKGMGIE LITTNWEALG QSVALYINSQ APGMQTLGAK PIRGFVQRLK GKQGRFRGNL
     SGKRVDFSGR TVIGPDPNLR IDEVAVPEKV AVKLSYPERV TDYNKAAMQD AIVNGSRLHP
     GANVLERRGD NGQPPMRIAL HVMKDREARK RWARDLQIGD IVHRHVRDGD IVLFNRQPSL
     HKLSIMCHRV RVRPWRTFRL NECVCNPYNA DFDGDEMNLH VPQTEEARTE ALELMSVKKN
     LVTPRNGEPI IAAIQDFITA SYLLSRRDRF FDRQQFAQIA SYLGDANLPI ELPPPVIWKP
     VRMWTGKQIF NLLMKPNKSS HVLVNLEAKC RTLVDPAKSD NFPPDMSPND GYLVIQNSEI
     MCGVFDKNTV GDGKKNSVFG VILRDYGPEE AAKAMNRLAK LSARFLANIG FSLGINDVIP
     GPVLFASKDA KVEKAYEECD EFIDLAKKGK LENAPGCDQE ATLEQKISGT LSAVREAVGK
     ICMQELSRHN APLIMATCGS KGSVINVAQM VACVGQQIIA GSRVPNGFQD RSLPHFRKKS
     KNPPSKGFVR NSFFSGLTPT EFLFHAISGR EGLVDTAVKT AETGYMARRL MKALEDLCTH
     YDLSVRNSVG GIVQFQYGDD MLDPACLEGD ATPVEYVRSW THACRTASRS GKALLPYEVR
     EIAQRIYPES KYRETTYNFI INKIVKTMVN QRVARGLPDA DDKAMAEEYE DLLVSEDRAI
     RQVLENANKV TEAQLNSFLE NCRIRYLRAK IEPGSTVGAV GAQSIGEPGT QMTLKTFHFA
     GVASMNVTLG VPRIKEIINA AKVISTPIIT AEMNIPESET AARIVKGRIE RTVLSDIASC
     IEESWTNANA YIEIHIDMKA VRRLQLEITL ESIKWSLVAA PKLKIPEGSI HISTKTSRIR
     VWIDEPPKDK EKNSGGIYER LKFLKRAIGD IQVKGLPSVD RGVVTKDEKN EKIHRLLVTG
     YGLSEVMGTE GVDGLKTKTN HVMETQKVLG IEAARSTIYN EIQHTMKSHG MSIDPRHVML
     LGDVMTYKGE VLGITRFGVQ KMKDSVLMLA SFEKTTDHLF DASLFSKKDE IQGVSECIIM
     GTPAPGCGTS LASIVTPAPI LPRKKPLLFE SAYKAGQDRI KSYNGLNHIN GNGMEIDVY
//
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