ID J9VSQ4_CRYNH Unreviewed; 1786 AA.
AC J9VSQ4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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_02166 {ECO:0000313|EMBL:AFR95654.1};
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:AFR95654.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR95654.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CP003825; AFR95654.1; -; Genomic_DNA.
DR RefSeq; XP_012049987.1; XM_012194597.1.
DR GeneID; 23885821; -.
DR KEGG; cng:CNAG_02166; -.
DR VEuPathDB; FungiDB:CNAG_02166; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000010091; Chromosome 6.
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:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_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; 3.30.1360.140; -; 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; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
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 Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 14.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 247..551
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1596..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 693..720
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1596..1629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1786 AA; 196182 MW; 5B6F1D2BE76FF647 CRC64;
MTVTFPYSSA PVKQVKEIQF GIMSPEEIKA FSVAKIESTE VLDENGKQKV GGLMDPKMGT
IDRNFKCQTC LEGMSECPGH FGHIELARPV FHQGFIVKVK KILECVCYSC GKLKVDMRDP
MVANAVRRIK AQHRLKAIWA LAKDKKICEP DELDEKDNGD ATFEDEYLQE QKAALKGHGG
CGHEQPVWRK KGLKLMGVWK PTDKGEDEAA EPEERNVSPG EVYNILKKIT PEDLHIMGLN
ADYARPDWMI LTVLPVPPAA VRPSIAVDGG AMRSEDDLTY KLSQIIKFNG VVRRMEAEGV
PPSVVNEQFD LLQYHVCTYM DNDIAGLPRD QQKGGRAIKA IRARLKGKEG RMRGNLMGKR
VDFSARTVIT GDPNLQLDQV GVPKSIAMTL TYPERVTPYN IVYLQTLVNN GPATYPGARY
YVKDTGERVD LKYRKSGEPI SLQFGWIVER HLKDGDYVLF NRQPSLHKMS MMSHRVKLMN
YSTFRLNLSV TSPYNADFDG DEMNLHVPQS EETRAELSQI AWVPRQIVSP QANKPVMGIV
QDTLCGIRKF TLRDNFLDWL QVQHILLWLP EWNGTIPPPA IFKPKPMWTG KQLLSMTIPK
GINITYKNNE KPSPIDVTDE NVLIENGELV HGTIVKNMAG SANNGLVHVI FRELGHIAAR
DFFSAVQRVV NYWLLHYGFS VGIGDTIVDK ATMAGITNRM VEAKEAVQKL IQEAEANRMK
PKPGMTIRET LEASIAAELN KARDWTGKTT QDNLKADNNV KQMVVSGAKG SFINISQMSG
VVGQQFVEGK RISFGFRHRS LPHFSRDDYG PESRGFVENS YLRGLTPQEF WFHAMGGREG
LIDTAVKTAE TGYIQRRLVK AMEDLKVAYD GTVRNSVNEV VQFLYGEDGM DGAAMEKQSL
DIIRLSDRAF ERRYKIDVLG GSGFSKGVLQ AGIDQSSISL QKLLDEEFAQ ISEDRRILRS
EIYPDGTPGH PLPVNIQRVI QNSQQIFHID PRVPSDLDPV YLLEQREALA DRLLVVRGDD
KLSRAAQKNA TLVFNMLLRS HLATRRVLEE YHLNREAFDW VIGEVEQIFN KAVVNAAEMV
GTLAAQSIGE PATQMTLNTF HYAGVASKSV TGGVPRLKEI INVAVNIRTP ALNVYLDPEY
SKTEEDAHQI MRKLTYTRLR DITATVEIFY DPKLDSTDIE EDKDFVDAFF AIPDEDIRLE
LHSPWLLRLE LDRAKVLEGG YEMSQIVDAI ADTVGKDVFV IHSEDNAPKL VIRIRVVAEK
EDEELLGDED MFLKRIEGTL LDQVELGGIT GITRVFISEG KQVVVSQNGE YDQEKEWFLE
TDGINLKAVM AVDGVNAFRT YSNNCYEVYE TLGIEAARNA LYKELNGVIE MGGSYVNYRH
LALLCDLMCS KGALMSITRH GINRTDAGAL SRAAFEETVE ILLEAAAVGD VDDCKGVAEN
VLLGQMAPMG TGAFDVSLDM NMLKDVIVDH RLPVQNMMAA GIAGGMTPGG AMTPYDNLSP
MWGGDKGALG HAAFSPIQSS ANDEGGNFAY MGYGQSPMHG GISPAGYSPS SPAGYSPTSP
FAVTSPAYSP TSPFAGAAAG GASPWVGRGG YGATSPAYSP TSPQYSPTSP QFSPTSPSFS
PSSPTYSPAS PAYGGAGAGN RASPYSPTSP AYSPTSPMGG ITSPQYSPTS PRYSPTSPAF
SPTSPSYSPT SPAPFQATSP RYSPTSPQFS PTSPTYSPAS PAYSPTSPQY SPTSPAYSPT
SPAYSPTSPT YGGAAPNGGT AQQQNGQARP GWGNTGGYGT SPSWKS
//