ID A0A177WL44_BATDL Unreviewed; 1811 AA.
AC A0A177WL44;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BDEG_23884 {ECO:0000313|EMBL:OAJ40111.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ40111.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ40111.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ40111.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ40111.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ40111.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-2016) 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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; DS022304; OAJ40111.1; -; Genomic_DNA.
DR STRING; 403673.A0A177WL44; -.
DR VEuPathDB; FungiDB:BDEG_23884; -.
DR eggNOG; KOG0262; Eukaryota.
DR Proteomes; UP000077115; 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:UP000077115};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 369..709
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 150..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1811 AA; 200925 MW; 7AF927A766F28513 CRC64;
MNISNPVSAE VRSVHFSFYS PQDLRKLSVK QITNPIIFDN LDHPTPQGLY DSALGPSGID
STCSTCSLGF SNCPGHFGHI ELSVPVYNSV NFKLLYKLLQ STCYYCHHLR TSRSVIHSFV
AKLKLIHAGL IVEAAELDSA LFSEPLINTS DSPKNSSSTN KSSTFINDEA EEDHEDMISK
SFMNVDTEDS EPQDSAGSVN FEKRTSAQII TAIDRFVDQA FAKNPYTRPS KVTLLTANIR
RLERQFFSAI PAQTCQNCRG QSPKFRKDGE SKIFEQPLNN KQKMSMNTQN LTPENLFGPK
MHAVDDDNEK TAQQGDAVSQ AIDSQREIFL TPLQVKAHIE LLWKRETVVL DLLFGNSSSK
KSPRVSSPLM FFLDVVSVTP NRFRPISKMG DSQYENPQNI FLTAILKANV SIQELQRQEE
AALKVIADDP KLYQLQKAEF LRRIIDAWMI LQNSVNYLLD SSKCPLSVSG KIAPPGIRQL
LEKKEGLFRK HMMGKRVNHA ARSVISPDPY IETNEIGIPP VFASKLTYPE PVTHHNIKEM
RRCVVNGPLK WPGATHVENE DGTLISLSSF DDAGRTAIAN QLLTPSMHHG ETNHSYNFDH
VNKKVYRHIR NGDFLLLNRQ PTLHKPSIMA HTARVLPGEK TIRMHYANCN TYNADFDGDE
MNIHFPQNEI ARAEAMLIAR NDQQYLVPTD GGVLRGLIQD HVDAGVDMCS RDTFFNRETY
MQLVYIGLCP EGSVTSTVGN GNIEPPIVIG RNGRVVTLPP AIIKPVAKWT GKQIISTILV
NLIPEDRNLL NLVSKSRIPA KQWGPSAPEE QTVIFMDGDL LTGILDKSQF GASANGLVHA
VYEVYGASYA GKLLSILGRL FTSYLQFAGF TCRMDDLRLT PEGDAVRCEL IESASSIGLD
AISEITGVNV EGISHDKRTM YMARSKGDKT ALAKNIELNV ALEQVLRNSE KMAALDSAMK
SRTNKVTSKI ISSCVPDRLL KPFPHNNMQV MTVSGAKGSG VNVSQISCLL GQQELEGKRV
PTMISGKTLP SFLAYDTSAR AGGYITGRFL TGIKPQEYYF HCMAGREGLI DTAVKTSRSG
YLQRCLIKHL EGLSVHYDHT VRDMDGSLLQ FQYGEDALDV VKQTTLQKFD FCALNYRALL
KRYDPSALAG KVDDESLERY LKKQRKQDRE SIRESGGSFK PNHDPILSIF SPSRHIGSVS
DGFADALSAY IEKNTSQLLY TSSSKKTHKN RTDENGEARP VKDTWSVPKI SARKFKVLME
LRYMHSLVEP GEAVGLLAAQ SIGEPSTQMT LNTFHFAGFG AKNVTLGIPR LREIIMTASQ
SIQTPLMRLP LKQEATVDQA HQIADQISRV VLSQIMHGVT VSETLVPKTP ERQKRVKQFC
VRLELWPQEA CQRQYGITDE DIGNIIEKKF VPILDRTIMR MLKVKFTGDN ASTEADEGQT
LASLGFTESS VEKTTKSSKP QNDGDEDESN GLDNGRSTNF KSSHSLIDRV VDAADLSDAE
GDDSEVSDDD GDNDATAVRQ NTKRQQQATY DGPDEDDEQV IEHLADIEMA NDDDKVSVNT
DPDSVNDADD GLDLDGFETE KHTNGINRSV RIQRASRFVS GYKFHKGSLR YCELTYELST
DTKKILMLPL VEEVCSNLIV RQVPGVSRCY YLPNESENDK SVNVGTDGVN LKGIWEYDNV
IDVNKIGTND IAAILHTYGV EAARAAIMQE IAGVFGVYGI QVDSRHLSII ADYMTFEGGY
KAFNRTCMGS NPSPFLQMSF ETTTSFLTTA TLTGDSDPLD SPSARIVMGQ AVKTGTGSFS
VLQPLVRSAR G
//
