ID J9VQT9_CRYNH Unreviewed; 1727 AA.
AC J9VQT9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=CNAG_01189 {ECO:0000313|EMBL:AFR94954.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94954.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR94954.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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}.
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DR EMBL; CP003824; AFR94954.1; -; Genomic_DNA.
DR RefSeq; XP_012049378.1; XM_012193988.1.
DR GeneID; 23884930; -.
DR KEGG; cng:CNAG_01189; -.
DR VEuPathDB; FungiDB:CNAG_01189; -.
DR HOGENOM; CLU_000487_2_4_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000010091; Chromosome 5.
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 Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 390..735
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1727 AA; 192038 MW; CDBD5707B57A5DBF CRC64;
MDISHSIHSE VSSLSFSFLS ADDIKAISVK KVDNPILLDN LNLPTRGGLY DPKLGPMGSR
DLCETCHLSY FACPGHFGHI ELPTPVYHPL FMNQCYHLLR GVCLYCHHFK MPEIVAASYV
ARLRLLDAGL LTESHEVAAL FDNAIGKSSR QKDNDEDEDA EGDVDMDAPA PQTIESAAEF
MVRIEAYVQH HLKLAKQNAG GRDSKVEDGY KDGLVFEERK KLLHEFGKKI WNRCTRCTAY
GNTFRKEKAI KIIEYDLTPK QKLANKLSNL RRPDVLAASG KYSSKQRRSD GDIDEGIEMD
SDKSSVSEGE GESLDEEEEE EQDVGQTVAK TASGQVKGTR GRHERVMSPA EVRAHLRLLF
GKEPEICRLI YGRHGNPAAL SSVAPPPLAD MFFMEVVPVT PTRFRPAARM GDELFENSQN
SLLTTVLSTC QRIQKLNQDL INQAKAERGE LVLDAVAKAQ GGRTFELLLE ALIKLQHDVN
SFVDSTKNPA VMRQGKLPPP GVKQLLEKKE GLFRKHMMGK RVNYAARSVI SPDINIETNE
IGIPPVFAKK LTYPEPVTQQ NVAELRQLVI NGPKIHPGAA LVQNEDGTQI SLDKLTLDQR
ISLANQLLTP QGSEDNIGAA SIGPAAKNKK VYRHIRDGDI VILNRQPTLH KPSMMCHRVK
VLLGEKTIRM HYANCNSYNA DFDGDEMNIH FPQNEVARAE AQMIANTDNQ YLVPTSGGPL
RGLIQDHVVA GVWMCNKSSF FTREQYFQLI YGALRTENNY TGRSRIITLP PAIFKPKPLW
TGKQIMSTIL TNLTPSNAQG LNLTSRNKVQ NKLWRRDDSS DPAMSEENVI FLDGHLVCGV
LDKSQYGASG YGLVHSVHEL YGPYVANRLL GVLSRLLTKY LQHDAFSCRM DDLILTAEGE
KIRKDILDKA SGDGAIAAMK YVGLPEGSKI EDPDTAKNLA IRLEEILRDD HLMAGLDAVM
QSAFNKTTSK INNDVLPDHL VRPFPDNNMQ MMTISGAKGS KVNASQISTL LGQQALEGRR
VPTMVSGKTL PSFKAFDTSA RAGGYVANRF LTGIRPQEYY FHCMAGREGL IDTAVKTSRS
GYLQRCLIKH LEGVKVHYDH TVRDSDSSVL QFLYGEDSLD VTKQTHLNKF DFAAANHLSL
LNKVRPGDTA GKVSDEALSH MKKALKKPHK HVPALSEYSP SRYIGSMSEA YAKKLNNYIE
DNKLGYIAKK GENKASPYTS ERVPEKEFLG LARARYMRSL VEPGEAVGLL ASQGVGEPST
QMTLNTFHLA GHGAANVTLG IPRLREIVMT ASSKPTTPTM KLPLREHISD KDIETFVKQV
SRLTLSEVVE RVTVTERLSS KSSESDSRQR KYTVLLEFYP PEEYGTEYEI TPEQLHESLA
WHFAPRLKKE IQNEIRRVAK TKEQEAQVGK GRKVRVGGDE GDEEEVDREP DVRRRGRDDE
LDNDDEDSYQ LKRAAQAKQH EYEADSDVDS GVADLEDFVE KELEEDDEED VEDDAAEKAK
KDQKADDWAE LFKLASKYAT TFSFDGHSGK SAQFDLEFPA SAPKLLLVDI IERTCRAAVV
HEIENIGRCM KIFSDKGEFT RSLITEGSNL RGMWALADEL VDLDRLSSND IYAILTTFGV
EAARRAIIDE VSSVFGAYGI AVDYRHLTII ADYMTHAGGF RPFNRTGISA KSSPLLKASF
ETTVAFLSEA TLHGDFDDLT SPAAKIVMGK PSASGTGAFD IRAPTRL
//
