ID A0A2P7YQF5_9ASCO Unreviewed; 1937 AA.
AC A0A2P7YQF5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=C7M61_002751 {ECO:0000313|EMBL:PSK38195.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK38195.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK38195.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK38195.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PSK38195.1}.
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DR EMBL; PYFQ01000006; PSK38195.1; -; Genomic_DNA.
DR STRING; 418784.A0A2P7YQF5; -.
DR EnsemblFungi; C7M61_002751_t1; PSK38195.1; C7M61_002751.
DR VEuPathDB; FungiDB:C7M61_002751; -.
DR OrthoDB; 169836at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd06855; GT_GPT_euk; 1.
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; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR033895; GPT.
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; PF00953; Glycos_transf_4; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 619..947
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 544..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1697
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1937 AA; 214943 MW; E6F82D56F91ED262 CRC64;
MNRLFYAGLV CLAAAIIKFD NPLQTLAGFG VLGFCFTTYL IPRLGPSFKK VGLQGKDLSK
IGPSEPIPES MGVVASITYM ILIVLIIPFV FFKYLVSYSS LSNDDDMLLN YKNQYKDYEN
KQLFPHNKLA EFLSAALCLL STIILGFFDD LFDIRWRHKF FLPAVASLPL LIVYYVDFSV
TSIVVPGFLM RNGVGEFFVI VLNQFSQKAN GLLTMLTGLK FTTLAIDYKI ESTAPRLLDL
GIFYYAYMSA LSIFCPNSIN ILAGINGLEV GQSIVLGAVL LINDLAYLLK FSKKPEFTMD
IAKPVGSEIS SVDFGVMSAD EIRRLSAKQI TNPIVFDNLG HPIANGLYDL ALGAFLRNLC
TTCGLDEHSC PGHQGHIELP VPVYNPLFLN QVFLFLRSSC LYCHQLRLNS LEVHKFACKL
QLIQYGLLLE CQELEDMLSQ DGSSADDGED GSKEHIPSDS RTVGLIKLKR EAFVEAAISS
ALSEGRTNAN GIVTETVGEV RKEVVGMFYK KILSRGKCEN CGMFSPTFRK DGAVKIFENS
LTDKQESSNR VKGGSRPDAL KKQPSQSSTS LGSKSKAGSK YVLLTEVRYI LRNVFKNEQV
VMQKIFHSRP SATAPVSADM FFIHSLIVPA TRFRLPSKLG DEIHENAQNE LLSNVLKTCL
LIRDLNDQIS ALFSKDKAAN SDSRKLLFNR LMNAFVTIQN DVNVFIDSTK NMNGSGGKQP
TPGIKQALEK KEGLFRKHMM GKRVNYAARS VISPDPNLET NEIGVPPVFA VKLTYPEPVT
SHNVSQLRQA VINGPDKWPG AIEVQNEDGY MTSLVGMTLE QRKTVANQLL TPSNGYSSLN
KKVYRHIKNN DVVVMNRQPT LHKASMMGHK VRVLPGEKTL RLHYANTGAY NADFDGDEMN
MHFPQNENAK SEALNLANTD SQYLTPTSGS PLRGLIQDHI SAGVWLTNKD TFFTREKYQQ
LIYGCIRPEH GHTNGSSRIL TVPPSIFKPE PLWTGKQVIT TILLNIKPKG VPGINLESKN
KVKNEYWGLG SQENSVIFKD GQLLCGILDK SQYGAAQYGI VHSLHEVYGP EVASKALSVL
GRLFTNYTLS TAFTCGMDDL RLTGEGNSWR NEILKKSVDI GRVAACEVTN LADDTANNDG
ELLKRLEEIL RDDGKLGILD AITQSKVNAI TSQVVGKCIP DGTMKRFPYN SMQAMALSGA
KGSGVNVSQI MCLLGQQALE GRRVPVMVSG KTLPSFKPFE TDARAGGYIK GRFYSGIRPQ
EYYFHCMAGR EGLIDTAVKT SRSGYLQRCL TKQLEGVHVA YDNSVRDGDG SLLQFLYGGD
AIDTTKQSHM NQFDFCLKNY DALVSRYNPG DLADHLDTDT ALSYAKKVRK QLKKVKLLKH
YDQNTKYDPV LSVFNPSKYL GSVSETFQDK LDDFSKQYPD LFSKNLASGV SEKKFKALMQ
LKYMRSLINP GEAVGIVAAQ SIGEPSTQMT LNTFHFAGHG AANVTLGIPR MREIIMTASA
SIATPQMSLP ILDDVDNSMA DSFCKLIGKV HLSEFIDDVT VTETTGIEEG NSTSYRSYKV
KMNFYSKNEY EGEYDISQNQ LEKVLSSKFL DKLELAINKN LKAQVNNSSK PSIGKAVPKA
QTDAALPTAS FQDETGDGDA TEEKLKSNSK QAVSYDEPDS DEVENMRKAE QTSEEELEET
DDSESESESE SEDESDGNLV NDEAKERKRT PRELTKSARD RQAEVISSHH FIKKYDFDDV
HGEWCEFEIE LLGNVQKLLM VNIIEDLCRG VVVREISNIG RCLRPQPDNG KRTLTTEGVN
FKAMWEQDDF IDVNAITSND IVSVLKTYGV EAARNTIVNE INNVFSTYAI SVSTRHLDLI
ADMMTREGTY RAFNRQGIDS STSAFKKMSY ETTCQFLTKA VLDGEREDLD SPSAKIVMGL
LSNVGTGSFD IMTNLEN
//
