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Database: UniProt
Entry: J9VSQ4_CRYNH
LinkDB: J9VSQ4_CRYNH
Original site: J9VSQ4_CRYNH 
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
//
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