ID F2PRD9_TRIEC Unreviewed; 1712 AA.
AC F2PRD9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=TEQG_03656 {ECO:0000313|EMBL:EGE04457.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995733; EGE04457.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TEQG_03656; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR Proteomes; UP000009169; 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: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; 2.
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; 2.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 10.
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; 3.
PE 3: Inferred from homology;
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 245..552
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 156..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1712 AA; 189289 MW; 7E5B4D85F0515B82 CRC64;
MSSVRFPYSK AQLRTIKEIQ FGLLSPEEIK RMSVCHVEYP ETMDDQRQRP REKGLNDPRL
GTIDRNWRCA TCEEGINDCP GHFGHIELST PVFHIGFLTK IKKLLETVCH NCGKIKANAS
DQKYLDALRF RDPKKRFDAI WRLSKDILIC EADPPEEDDP FAKESSKPVQ GHGGCGNVQP
QVRKEGITLM GTWKPSKMRD MMDDNEIQQP EKKQITPQMA LTIFRNISEE DVRLMGLSND
YARPEWMIIT VLPVPPPPVR PSVLVGGSGT GQRGEDDLTY KLAEIIRANQ NVTRCEQEGS
PEHVVREFES LLQYHVATYM DNDIAGIPQA MQKSNRPVKA IRGRLKGKEG RLRQNLMGKR
VDFSARTVIT GDPNLSLDEV GVPISIAQTL TYPEVVTPYN IHRLGQLVDN GPDVHPGARH
VIRSSGERID LRHHKGGGGR NFLQWGWKVE RHLMDGDFIL FNRQPSLHKE SMMSHRVRVM
PYSTFRLNLS VTTPYNADFD GDEMNLHVPQ SEEARAELNQ LCLVPLNIVS PQRNGPLMGI
VQDTLCGIYK ICRRDVFLTK EQVMNVLLWV PDWDGVLPQP AILKPRPRWS GKQMISMVLP
SGLNLLRIDK DKSPISEKFS PLADGGVLVH GGELMYGMFS KKTVGASGGG VVHTIFNEYG
PDAAMSFFNG AQAVVNYWLL HNGFSIGIGD TIPDLETIQK IENAVRVRKE EVDSITASAT
ENTLEALPGM NVRETFESKV SRALNNARDE AGTATEKSLK DSNNAVQMAR SGSKGSTINI
SQMTAVVGQQ SVEGKRIPFG FKYRTLPHFT KDDYSPESRG FVENSYLRGL TPTEFFFHAM
AGREGLIDTA VKTAETGYIQ RKLVKALEEV MVKYDGTVRN SLGDIVQFLY GEDGLDGQCI
ENQRVDVIKC SDEQFRNRFR VDLMDPERLL SPDILEQATE IAGDIEVQKH LDEEWEQLLK
DRAFLRTVVK EDDEMMQLPI NIQRILESAK TTFRIRDGTI SDLHPAEVVP QVRQLLDRLL
VVRGDDALSR EAQESATLLF KAQLRSRLAF RRLVVEYSLN KLAFQHVLGA IESRFGKAAA
NPGEMVGVPR LKEILNVATN IKTPSMTVYQ APECRMNKES AKQLRSIVEH TSLRSVTEST
EIYYDPNIQS TVIENDVDMV ESYFIIPEDV ADDSSRQSKW LLRIILSRPK LLDKGLTVQD
VATKIKEAYP QDIAVIFSDN NADEQVVRIR QIQDPKQDED DDDTEYDVTL KKLESHLLDT
LTLRGVPGID RAFINEKSRT RVLEDGSLHQ SASDPECKEW VLETSGSALA DVLAIPGIDA
SRTYSNQFVE ILEVFGIEAT RTALLRELTQ VLAFDGSYVN HRHLALLVDV MTSRGFLMAV
TRHGINRADT GALMRCSFEE TVEILLDAAA FAELDDCRGV SENLILGQMA PAGTGEFDVY
LDQSMLMGVV SNNAGLGAMG EEPKGMLSDG AATQYDSGSP MQENMYISSP DPDSQFSPVR
QAGSENTVGF ADYQPPSYGG FSPHEPRSPG GGYSPSSPFN TSPTSPAYSP SSGYSPTSPG
MSITSPRFIS SPAFSPASPS FAPTSPAYSP TSPGYGQAQS PTSPSYSPTS PGFSPTSPSY
SPTSPSFSPA SPVFSPTSPS YSPTSPALGG TGRHLSPTSP TSPKYTPTSP GWSPTSPEAY
SPTSPNFSGS PTSPGGPTSP GYSPTSPTFN PT
//
