ID A8QBY2_MALGO Unreviewed; 1673 AA.
AC A8QBY2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=MGL_3952 {ECO:0000313|EMBL:EDP41744.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP41744.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP41744.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP41744.1}.
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DR EMBL; AAYY01000016; EDP41744.1; -; Genomic_DNA.
DR RefSeq; XP_001728958.1; XM_001728906.1.
DR STRING; 425265.A8QBY2; -.
DR GeneID; 5853264; -.
DR KEGG; mgl:MGL_3952; -.
DR VEuPathDB; FungiDB:MGL_3952; -.
DR InParanoid; A8QBY2; -.
DR OMA; NREDYQQ; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000008837; 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; 6.10.250.2940; -; 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:UP000008837};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 302..664
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 88..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1673 AA; 186177 MW; 4FF3D6547DC1A809 CRC64;
MNHFECPGHF GHIELPAPVF HPLFMNHAYS LLRGTCLYCH HFKISKMALA KYTAQFHLLE
YGLVDEAERI ANEQFRGPHS AGVDVVEEGA NEDGDDDDDE PLAQLQNDNQ PAETVDDFIR
RIRQAVHRLT AQARKCGIRR NADKGMATYS ARRDLRNLFL KDIMRRRCER CQAINPTLRK
DGFVKITERD LSARDHAIHE ARGIKRQNVL MDRASTMTVR DTNGQTIRAA GNEPDSESTI
ETAITLKEAR KLSKEAGDHT RVVPASECRA NLRRLFANES EICSLIFGRH PMFGSTPAPS
ADVFFLEVIC VTPTRFRPAS VMGDQTFENP QNELLTKILN TAFFVRDCNE RAQVYQTKAN
YPVLDEMNEQ QAITAQKQWE MDRRAAMDQL LSAIMQLQVS VNCYMDSSKN PAPQRQGQAA
TPGVKQGLEK KEGLFRKHMM GKRVNFAARS VISPDVNIET NEIGVPPVFA KRLTYPEPVT
VHNYELMRQL VINGPDVYPG AHAVRGEDGT DTLLKNLSVE ERTALANQLL TPQGQTSRQA
RGTFGGIGGT LRTPVINKQV LRHLRTGDIL VMNRQPTLHK PSMMAHRARV LQGERTIRMH
YANCNSYNAD FDGDEMNMHF PQSQMARAEC YNIANTDNQY LVPTSGNPLR GLIQDHVVGG
VWMTCKNTLY TRDEYQQFIF GAIRPETYGQ GGRIRTLPPA ILKPKPRWTG KQVISTILCN
VTPPHAQGLN MDAKARVGAK YWGEQHKEEE MVVVRDGELL TGVLDKSQIG ASAYGLVHAV
YEIYGAESAG RLLSIFSRLF TMWLQHNAFS CRMDDLVLSS EGDATRQKIL KDGATHGLEA
ALNNVGLGDG DSKAPETHRN LRVRLEEVLR DDNKLAALDA AMMSASNKLT SSVISSCIPS
GLWRVFPENN MQMMAVSGAK GSAVNVSSIS CLLGPQALEG RRVPVMVSGK TLPSFKAFET
AARAGGFVAG RFLTGIAPQE YYFHCMAGRE GLIDTAVKTS RSGYLQRCLI KHLEGISVQY
DQTVRNSDGF VLQFHYGEDS LDVSKSKYLD RFDFTIQNFE SYRRRYNPVQ LESTMEVEKA
PDYMKRALKK PYKYAPVMSV YSPARHFGSM SETFAQKVED YVSKNPRALL ARKKKDSASE
GVPMQLAHPK LSTEAFRAMT KVLYHRGLVE PGENVGLLAA QGIGEPSTQM TLNTFHFAGH
GAANVTLGIP RLREIVMTAS KDIKTPVMRL PILDGVTNEQ MRIFCKDGSR LVLSQIIEEA
TVTERMMPKT PANGYQRQKL YTVRLQFYPA DEVKQEYNAS TEHILSGLEA TFVPLVEREI
VRELKRLRRD QVRQSQSIGR GETFNESMAE RDADVPIYRN AAANDSDDED ERLSEAGDDD
DDATAAKRRA NAGSKVSYDD AADAEDDRAK DTTDDITRAF NDADDIEDGD EQALSAQKDV
GDEAIDARVT ELDERLQNES KFVVSFRFDS VAGAWAEFDL QMLNSTEKML LINVIERVCR
ASVVHEIPRI SRIMIPPPVP GDPSVALTAE GINLPGMWDF GFGVVDLDRI YSNDIGALLY
CYGVEAARAA IVSELKGIFD TYGIGVSMRH MFLIADYQTA FGDFRPFSRG GLADAPSPLL
KASFEMTMAF LSGASLFQEM DDLTSPSSNI VVGRPVRSGT GATTVHLPLA AAA
//
