(data stored in ACNUC11299 zone)

SWISSPROT: C4R4Y0_KOMPG

ID   C4R4Y0_KOMPG            Unreviewed;      1743 AA.
AC   C4R4Y0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 48.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   OrderedLocusNames=PAS_chr3_0568 {ECO:0000313|EMBL:CAY70616.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia
OS   pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70616.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY70616.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
RN   [2] {ECO:0000213|PDB:5X4Z, ECO:0000213|PDB:5X50, ECO:0000213|PDB:5X51}
RP   X-RAY CRYSTALLOGRAPHY (4.29 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=28412353; DOI=10.1016/j.bbrc.2017.04.039;
RA   Ehara H., Umehara T., Sekine S.I., Yokoyama S.;
RT   "Crystal structure of RNA polymerase II from Komagataella pastoris.";
RL   Biochem. Biophys. Res. Commun. 487:230-235(2017).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000256|RuleBase:RU004279}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000256|RuleBase:RU004279}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|RuleBase:RU004279}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FN392321; CAY70616.1; -; Genomic_DNA.
DR   RefSeq; XP_002492795.1; XM_002492750.1.
DR   PDB; 5X4Z; X-ray; 7.80 A; A/M=1-1743.
DR   PDB; 5X50; X-ray; 4.29 A; A=1-1743.
DR   PDB; 5X51; X-ray; 7.00 A; A/M=1-1743.
DR   PDBsum; 5X4Z; -.
DR   PDBsum; 5X50; -.
DR   PDBsum; 5X51; -.
DR   SMR; C4R4Y0; -.
DR   STRING; 644223.XP_002492795.1; -.
DR   EnsemblFungi; CAY70616; CAY70616; PAS_chr3_0568.
DR   GeneID; 8199932; -.
DR   KEGG; ppa:PAS_chr3_0568; -.
DR   eggNOG; KOG0260; Eukaryota.
DR   eggNOG; COG0086; LUCA.
DR   HOGENOM; HOG000222975; -.
DR   InParanoid; C4R4Y0; -.
DR   KO; K03006; -.
DR   OMA; MPDFDPT; -.
DR   OrthoDB; EOG092C01XQ; -.
DR   Proteomes; UP000000314; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:InterPro.
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; 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   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; 15.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 3.
PE   1: Evidence at protein level;
DR   PRODOM; C4R4Y0.
DR   SWISS-2DPAGE; C4R4Y0.
KW   3D-structure {ECO:0000213|PDB:5X4Z, ECO:0000213|PDB:5X50,
KW   ECO:0000213|PDB:5X51};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000314};
KW   DNA-directed RNA polymerase {ECO:0000256|RuleBase:RU004279};
KW   Metal-binding {ECO:0000213|PDB:5X4Z, ECO:0000213|PDB:5X50,
KW   ECO:0000213|PDB:5X51};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU004279};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW   Transcription {ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|RuleBase:RU004279};
KW   Zinc {ECO:0000213|PDB:5X4Z, ECO:0000213|PDB:5X50,
KW   ECO:0000213|PDB:5X51}.
FT   DOMAIN      233    536       RPOLA_N. {ECO:0000259|SMART:SM00663}.
FT   METAL        67     67       Zinc 1. {ECO:0000213|PDB:5X4Z}.
FT   METAL        67     67       Zinc 2. {ECO:0000213|PDB:5X50}.
FT   METAL        70     70       Zinc 1. {ECO:0000213|PDB:5X4Z}.
FT   METAL        70     70       Zinc 2. {ECO:0000213|PDB:5X50}.
FT   METAL        70     70       Zinc 3. {ECO:0000213|PDB:5X4Z}.
FT   METAL        77     77       Zinc 3. {ECO:0000213|PDB:5X4Z}.
FT   METAL        80     80       Zinc 1; via tele nitrogen.
FT                                {ECO:0000213|PDB:5X4Z}.
FT   METAL        80     80       Zinc 3; via tele nitrogen.
FT                                {ECO:0000213|PDB:5X4Z}.
FT   METAL       107    107       Zinc 4. {ECO:0000213|PDB:5X4Z,
FT                                ECO:0000213|PDB:5X51}.
FT   METAL       107    107       Zinc 5. {ECO:0000213|PDB:5X50}.
FT   METAL       110    110       Zinc 4. {ECO:0000213|PDB:5X4Z,
FT                                ECO:0000213|PDB:5X51}.
FT   METAL       148    148       Zinc 4. {ECO:0000213|PDB:5X4Z,
FT                                ECO:0000213|PDB:5X51}.
FT   METAL       167    167       Zinc 5; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:5X50}.
FT   METAL       168    168       Zinc 5. {ECO:0000213|PDB:5X50}.
SQ   SEQUENCE   1743 AA;  193897 MW;  C61FD1B6AFF25C54 CRC64;
     MSQFPYSSAP LRSVKEVQFG LLSPEEIRAI SVVKIEYPEI MDESRQRPRE GGLNDPKLGS
     IDRNFKCQTC GEGMAECPGH FGHMELAKPV FHIGFIPKIK KVCECICMNC GKLLLDETNP
     TMAQAIRIRD PKKRFNAVWQ LCKTKMVCEA DAPVDEYSEQ KVVSRGGCGN TQPVVRKDGM
     KLWGTWKKSG FSDRDAQPER KLLTPGEILN VFKHISPEDC FRLGFNEDYA RPEWMIITVL
     PVPPPQVRPS IAMDETTQGQ DDLTHKLSDI LKANINVQKL EMDGSPQHII NEVEQLLQFH
     VATYMDNDIA GQPQALQKSG RPVKAIRARL KGKEGRLRGN LMGKRVDFSA RTVISGDPNL
     ELDQVGVPIS IAKTLSYPET VTQYNIHRLT EYVRNGPNEH PGAKYVIRDN GDRIDLRYHK
     RAGDIVLQYG WKVERHLMDD DPVLFNRQPS LHKMSMMAHR VKVMPYSTFR LNLSVTSPYN
     ADFDGDEMNL HVPQSEETRA ELSQLCAVPL QIVSPQSNKP VMGIVQDTLC GVRKMTLRDT
     FIEYEQVMNM LFWVPSWDGV VPQPAILKPK PLWTGKQLLS IAIPSGIHLQ RTDGGNSLLS
     PKDNGMLIVD GKVMFGVVDK KTVGSGGGGL IHTVMREKGP KICAELFGNI QKVVNYWLLH
     NGFSIGIGDA IADASTMKEI THAISSAKEQ VQEIIYKAQH NELELKPGMT LRESFEGEVS
     RTLNDARDSA GRSAEMNLKD LNNVKQMVSA GSKGSFINIA QMSACVGQQM VEGKRIAFGF
     ADRSLPHFTK DDFSPESKGF VENSYLRGLT PQEFFFHAMA GREGLIDTAV KTAETGYIQR
     RLVKALEDIM VHYDGTTRNS LGDIIQFLYG EDGLDGTQVE RQTIDTIPGS DKAFHKRYYV
     DLMDEKNSIK PDVIEYAADI LGDVELQKEL NSEYEQLVSD RKFLREIVFV NGDHNWPLPV
     NLRRIIQNAQ QIFHLDRAKA SDLTIPEIIH GVRDLCKKLF VLRGENELIK EAQQNATSLF
     QCLVRARLAT RRILEEFRLN RDAFEWVLGT IEAQFQRSLV HPGEMVGVIA AQSIGEPATQ
     MTLNTFHYAG VSSKNVTLGV PRLKEILNVA KNIKTPALTV YLDREIALDI EKAKVIQSSI
     EYTTLKNVTS ATEIYYDPDP TSTVIEEDFD TVEAYFSIPD EKVEETIDKQ SPWLLRLELD
     RARMLDKQLT MNQVADKISE VFSDDLFVMW SEDNADKLII RCRVIRDPKA MDEELEAEED
     QMLKRIEAHM LDLIALRGIP GISKVYMVKH KVSVPDESGE YKNEELWALE TDGINLAEVM
     AVPGVDSSRT YSNSFVEILS VLGIEATRSS LYKEILNVIA FDGSYVNYRH MALLVDVMTS
     RGYLMAITRH GINRADTGAL MRCSFEETVE ILFEAGAAAE LDDCRGVSEN VMLGQLAPMG
     TGAFDVMIDE KLLTSLPADY APTMPLFKGK ATQGSATPYD NNAQYDDEFN HDDVADVMFS
     PMAETGSGDD RSGGLTEYAG IQSPYQPTSP GLSATSPGFA PTSPGFAPTS PRYSPTSPGY
     SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
     PSYSPTSPQY SPTSPQYSPT SPQYSPTSPQ YSPTSPQYSP TSPQYSPTSP QYSPTSPQYS
     PTSPQYSPTS PQYSPTSPQY SPTSPQYSPT SPQYSPTSPQ YSPASPQYSP SRHSPNGESK
     EGE
//

If you have problems or comments...

PBIL Back to PBIL home page