ID A0A1E3HZ95_9TREE Unreviewed; 1732 AA.
AC A0A1E3HZ95;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=L202_02070 {ECO:0000313|EMBL:ODN81672.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN81672.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN81672.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN81672.1,
RC ECO:0000313|Proteomes:UP000094065};
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 (JUN-2016) 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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN81672.1}.
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DR EMBL; AWGJ01000003; ODN81672.1; -; Genomic_DNA.
DR RefSeq; XP_018995991.1; XM_019135588.1.
DR STRING; 1295533.A0A1E3HZ95; -.
DR GeneID; 30153379; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000094065; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.357.120; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
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; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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:UP000094065};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 395..739
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 279..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1732 AA; 192833 MW; D52091A65BCB09AF CRC64;
MDIAHSLHSE IDSLSFSFLS TEDVQAISVK KLDNPILLDN FNLPTRGGLY DPKLGPMSAR
DVCETCHLSF YACPGHYGHI ELPVPVYHPL FMNQCYGLLR GVCLYCHHFK MPEVTLASYA
ARLRLLDAGL LTESHEVAAQ FDNAVGKSAR SKDKDAEEDI EGDVDMEEVA ATQAPENVAE
FLVRIEAYVQ HHLKTAKHNA ANKKRAEDAY KDGLVFEERK KLLHEFGKKI WNKCSRCHAY
GNTFRKEKAI KIIEYDLTPK QKLSNKLANL RRPDVLASAG KYSSKQRRSD DAAEVDEGIE
MDSDKSNSSD EEGEDVASDA EEEGDNEDVA HKVAKTASGQ VKGTRGRNER VMSPAEVRAH
LRLLFKKEPQ ICKIIYGKHG SPSASAFFSP APLADMFFMS VLPVTPTRFR PAARMGDDLF
ENSQNSLLTA VMQTCQRIQK LNQGLIDQAR AERGEIELDE VAKAQAPRTF ELLLETLIKI
QHDVNSFVDS TKNPAVMRQG KLPPPGIKQL LEKKEGLFRK HMMGKRVNYA ARSVISPDIN
IETNEIGIPP VFAKKLTYPE PVTQQNVAEL RQLVINGPKN HPGASLVQNE DGTQISLDRT
TVAQRTAIAN QLLTPQGDDH GLGGSAGPSK KNKKVYRHIR DGDIVILNRQ PTLHKPSMMC
HRVKVLLGEK TIRMHYANCN SYNADFDGDE MNIHFPQNEV ARAEAMMIAN TDNQYLGPTS
GSPLRGLIQD HVVAGVWMCN KSSFFTREQY FQLIYGALRT ENDYTGRSKI MTLPPAIFKP
RPMWTGKQIM STILLNLTPN NARGLNLTSR NKVQNKLWQR DDSSDPTMSE ENVIFLDGHL
ICGVLDKSQY GASGYGLVHS VHELYGPYIA NKLLGVLSRC LTKYLQHNAF SCRMDDLILT
AEGEKIRKDI LDKASGDGAT AAMKYVGLPE NSRIEDPDTA KNLAIRLEEI LRDDHLMAGL
DAVMQSAFNK TTSKINNDVL PEHLVRPFPD NNMQMMTISG AKGSKVNASQ ISTLLGQQAL
EGRRVPTMVS GKTLPAFKAF DTSARAGGYV ANRFLTGIRP QEYYFHCMAG REGLIDTAVK
TSRSGYLQRC LIKHLEGVKV HYDHTVRDSD SSVLQFLYGE DSLDVTKQTH LNKFDFAAAN
HTSLVQKVRP NDVSSKVNHE APGLMKKALK KPHKYPPVLS EYSPSRYIGA MSEAYAKKLD
SYIEDNKFGY ISKKNDNKAS PFTSERVPEK EFMHLARARY MRSLVEPGEA VGLMASQGVG
EPSTQMTLNT FHLAGHGAAN VTLGIPRLRE IVMTASAKPT TPTMKLPLRD QISDKDIETF
VKQVSRLTLS EVVERVTVTE RLSAKSGEND SRQRKYTVLL EFFPLKEYTS EYEITPEQLH
ESLAFNFAPK LKKEIQNEIR KVAKTKEQEL QVGKGRKVRA GGEDGGEEEE REPEVRRRGR
DDELDDDDED SYQLKRTAQA RQHEYEEDSD GGDSGVADLE DILENDLEGE DDEDVDEEGA
TEKAKQDSKA DDLAELFKLG SKYATTFSFD NHGGKSAQFD LEFPANAPKL LLVDLIERTC
RSAVVHEIEN IGRCMKIFSD KGEFTRSLIT EGSNLRGMWA LADELVDLDK LSSNDIYAIL
TTFGVEAARK AIIDEVSSVF GAYGIAVDYR HLTIIADYMT HGGGYRPFNR TGIAAKSSPL
LKASFETTVA FLSEATLHGD FDDLTSPAAK IVMGKPSSSG TGAFDIRAPT RI
//