NRPB1_ARATH
ID NRPB1_ARATH Reviewed; 1839 AA.
AC P18616; P31635; Q56Z04; Q9SZS8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB1 {ECO:0000303|PubMed:19110459, ECO:0000303|PubMed:2103447};
DE Short=DNA polymerase II subunit B1 {ECO:0000303|PubMed:19110459, ECO:0000303|PubMed:2103447};
DE EC=2.7.7.6 {ECO:0000269|PubMed:19110459};
DE AltName: Full=DNA-directed RNA polymerase II largest subunit {ECO:0000303|PubMed:16497658};
DE AltName: Full=DNA-directed RNA polymerase II subunit 1 {ECO:0000303|PubMed:2103447};
GN Name=NRPB1 {ECO:0000303|PubMed:19110459};
GN Synonyms=RPB1 {ECO:0000303|PubMed:2103447},
GN RPB205 {ECO:0000303|PubMed:2259344}, RPII {ECO:0000303|PubMed:16497658,
GN ECO:0000303|PubMed:2103447};
GN OrderedLocusNames=At4g35800 {ECO:0000312|Araport:AT4G35800};
GN ORFNames=F4B14.70 {ECO:0000312|EMBL:CAA21466.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2259344; DOI=10.1007/bf00315798;
RA Nawrath C., Schell J., Koncz C.;
RT "Homologous domains of the largest subunit of eucaryotic RNA polymerase II
RT are conserved in plants.";
RL Mol. Gen. Genet. 223:65-75(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2103447; DOI=10.1007/bf00036908;
RA Dietrich M.A., Prenger J.P., Guilfoyle T.J.;
RT "Analysis of the genes encoding the largest subunit of RNA polymerase II in
RT Arabidopsis and soybean.";
RL Plant Mol. Biol. 15:207-223(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1743-1839.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH CYP59.
RX PubMed=16497658; DOI=10.1261/rna.2226106;
RA Gullerova M., Barta A., Lorkovic Z.J.;
RT "AtCyp59 is a multidomain cyclophilin from Arabidopsis thaliana that
RT interacts with SR proteins and the C-terminal domain of the RNA polymerase
RT II.";
RL RNA 12:631-643(2006).
RN [7]
RP INTERACTION WITH PRP40A; PRP40B AND PRP40C.
RX PubMed=19467629; DOI=10.1016/j.abb.2009.01.004;
RA Kang C.H., Feng Y., Vikram M., Jeong I.S., Lee J.R., Bahk J.D., Yun D.J.,
RA Lee S.Y., Koiwa H.;
RT "Arabidopsis thaliana PRP40s are RNA polymerase II C-terminal domain-
RT associating proteins.";
RL Arch. Biochem. Biophys. 484:30-38(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP AND NOMENCLATURE.
RX PubMed=19110459; DOI=10.1016/j.molcel.2008.12.015;
RA Ream T.S., Haag J.R., Wierzbicki A.T., Nicora C.D., Norbeck A.D., Zhu J.K.,
RA Hagen G., Guilfoyle T.J., Pasa-Tolic L., Pikaard C.S.;
RT "Subunit compositions of the RNA-silencing enzymes Pol IV and Pol V reveal
RT their origins as specialized forms of RNA polymerase II.";
RL Mol. Cell 33:192-203(2009).
RN [9]
RP INTERACTION WITH RDM1, AND SUBCELLULAR LOCATION.
RX PubMed=20410883; DOI=10.1038/nature09025;
RA Gao Z., Liu H.L., Daxinger L., Pontes O., He X., Qian W., Lin H., Xie M.,
RA Lorkovic Z.J., Zhang S., Miki D., Zhan X., Pontier D., Lagrange T., Jin H.,
RA Matzke A.J., Matzke M., Pikaard C.S., Zhu J.K.;
RT "An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA
RT methylation.";
RL Nature 465:106-109(2010).
RN [10]
RP PHOSPHORYLATION, INTERACTION WITH ATX1, AND SUBUNIT.
RC STRAIN=cv. Wassilewskija;
RX PubMed=21266657; DOI=10.1105/tpc.110.080150;
RA Ding Y., Avramova Z., Fromm M.;
RT "Two distinct roles of ARABIDOPSIS HOMOLOG OF TRITHORAX1 (ATX1) at
RT promoters and within transcribed regions of ATX1-regulated genes.";
RL Plant Cell 23:350-363(2011).
RN [11]
RP INTERACTION WITH MEE12/CCG1 AND ME14/CBP1.
RX PubMed=26462908; DOI=10.1105/tpc.15.00370;
RA Li H.J., Zhu S.S., Zhang M.X., Wang T., Liang L., Xue Y., Shi D.Q., Liu J.,
RA Yang W.C.;
RT "Arabidopsis CBP1 is a novel regulator of transcription initiation in
RT central cell-mediated pollen tube guidance.";
RL Plant Cell 27:2880-2893(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic component of RNA polymerase II which synthesizes
CC mRNA precursors and many functional non-coding RNAs. Forms the
CC polymerase active center together with the second largest subunit. Pol
CC II is the central component of the basal RNA polymerase II
CC transcription machinery. It is composed of mobile elements that move
CC relative to each other. NRPB1 is part of the core element with the
CC central large cleft, the clamp element that moves to open and close the
CC cleft and the jaws that are thought to grab the incoming DNA template.
CC At the start of transcription, a single-stranded DNA template strand of
CC the promoter is positioned within the central active site cleft of Pol
CC II. A bridging helix emanates from NRPB1 and crosses the cleft near the
CC catalytic site and is thought to promote translocation of Pol II by
CC acting as a ratchet that moves the RNA-DNA hybrid through the active
CC site by switching from straight to bent conformations at each step of
CC nucleotide addition. During transcription elongation, Pol II moves on
CC the template as the transcript elongates. Elongation is influenced by
CC the phosphorylation status of the C-terminal domain (CTD) of Pol II
CC largest subunit (NRPB1), which serves as a platform for assembly of
CC factors that regulate transcription initiation, elongation, termination
CC and mRNA processing. {ECO:0000269|PubMed:19110459}.
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:0000269|PubMed:19110459};
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of at least 12 subunits. Interacts with RDM1. Interacts (via CTD) with
CC PRP40A, PRP40B, PRP40C and CYP59 (PubMed:16497658, PubMed:19110459,
CC PubMed:19467629, PubMed:20410883). Interacts with MEE12/CCG1 and
CC MEE14/CBP1 (PubMed:26462908). Binds (via CTD) to ATX1, especially when
CC phosphorylated on 'Ser-5' of the heptapeptide repeat (PubMed:21266657).
CC {ECO:0000269|PubMed:16497658, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:19467629, ECO:0000269|PubMed:20410883,
CC ECO:0000269|PubMed:21266657, ECO:0000269|PubMed:26462908}.
CC -!- INTERACTION:
CC P18616; Q6Q151: CYP59; NbExp=3; IntAct=EBI-1540537, EBI-1625989;
CC P18616; Q9LUJ3: RDM1; NbExp=2; IntAct=EBI-1540537, EBI-15850569;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20410883}. Note=Peri-
CC nucleolar. {ECO:0000269|PubMed:20410883}.
CC -!- DOMAIN: The C-terminal domain (CTD) serves as a platform for assembly
CC of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. {ECO:0000305}.
CC -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can
CC be highly phosphorylated. The phosphorylation activates Pol II.
CC Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the
CC heptapeptide repeat. The phosphorylation state is believed to result
CC from the balanced action of site-specific CTD kinases and phosphatase,
CC and a 'CTD code' that specifies the position of Pol II within the
CC transcription cycle has been proposed. ATX1 seems to regulate
CC phosphorylation statment (PubMed:21266657). 'Ser-2' and 'Ser-5'
CC phosphorylation are repressed by flavopiridol (Flap) and seliciclib
CC (Selic), inhibitors of CDK7 and CDK9 (PubMed:21266657).
CC {ECO:0000269|PubMed:21266657}.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion temporarily coordinated by three conserved
CC aspartate residues of the two largest RNA Pol II subunits. The
CC ribonucleoside triphosphate is transferred by a rotation to the
CC nucleotide addition (A) site for pairing with the template DNA. The
CC catalytic A site involves three conserved aspartate residues of the RNA
CC Pol II largest subunit which permanently coordinate a second magnesium
CC ion. {ECO:0000305|PubMed:19110459}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36735.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X52954; CAA37130.1; -; Genomic_DNA.
DR EMBL; X52494; CAA36735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031986; CAA21466.2; -; Genomic_DNA.
DR EMBL; AL161588; CAB81489.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86573.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67520.1; -; Genomic_DNA.
DR EMBL; AK221166; BAD95215.1; -; mRNA.
DR PIR; G85422; G85422.
DR PIR; T04690; JDMU1.
DR RefSeq; NP_001329346.1; NM_001342374.1.
DR RefSeq; NP_195305.2; NM_119746.4.
DR AlphaFoldDB; P18616; -.
DR SMR; P18616; -.
DR BioGRID; 15016; 35.
DR DIP; DIP-40008N; -.
DR IntAct; P18616; 4.
DR MINT; P18616; -.
DR STRING; 3702.AT4G35800.1; -.
DR iPTMnet; P18616; -.
DR PaxDb; P18616; -.
DR PRIDE; P18616; -.
DR ProteomicsDB; 249447; -.
DR EnsemblPlants; AT4G35800.1; AT4G35800.1; AT4G35800.
DR EnsemblPlants; AT4G35800.2; AT4G35800.2; AT4G35800.
DR GeneID; 829734; -.
DR Gramene; AT4G35800.1; AT4G35800.1; AT4G35800.
DR Gramene; AT4G35800.2; AT4G35800.2; AT4G35800.
DR KEGG; ath:AT4G35800; -.
DR Araport; AT4G35800; -.
DR TAIR; locus:2125319; AT4G35800.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR InParanoid; P18616; -.
DR OMA; KSAPCMG; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; P18616; -.
DR PRO; PR:P18616; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P18616; baseline and differential.
DR Genevisible; P18616; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
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; PTHR19376; 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 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; 23.
PE 1: Evidence at protein level;
KW DNA-binding; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transferase; Zinc.
FT CHAIN 1..1839
FT /note="DNA-directed RNA polymerase II subunit RPB1"
FT /id="PRO_0000073933"
FT REPEAT 1544..1550
FT /note="1"
FT REPEAT 1551..1557
FT /note="2"
FT REPEAT 1558..1564
FT /note="3"
FT REPEAT 1565..1571
FT /note="4"
FT REPEAT 1572..1578
FT /note="5"
FT REPEAT 1579..1585
FT /note="6"
FT REPEAT 1586..1592
FT /note="7"
FT REPEAT 1593..1599
FT /note="8"
FT REPEAT 1600..1606
FT /note="9"
FT REPEAT 1607..1613
FT /note="10"
FT REPEAT 1614..1620
FT /note="11"
FT REPEAT 1621..1627
FT /note="12"
FT REPEAT 1628..1634
FT /note="13"
FT REPEAT 1635..1641
FT /note="14"
FT REPEAT 1642..1648
FT /note="15"
FT REPEAT 1649..1655
FT /note="16"
FT REPEAT 1656..1662
FT /note="17"
FT REPEAT 1663..1669
FT /note="18"
FT REPEAT 1670..1676
FT /note="19"
FT REPEAT 1677..1683
FT /note="20"
FT REPEAT 1684..1690
FT /note="21"
FT REPEAT 1691..1697
FT /note="22"
FT REPEAT 1698..1704
FT /note="23"
FT REPEAT 1705..1711
FT /note="24"
FT REPEAT 1712..1718
FT /note="25"
FT REPEAT 1719..1725
FT /note="26"
FT REPEAT 1726..1732
FT /note="27"
FT REPEAT 1733..1738
FT /note="28; approximate"
FT REPEAT 1739..1745
FT /note="29"
FT REPEAT 1752..1758
FT /note="30"
FT REPEAT 1759..1765
FT /note="31"
FT REPEAT 1766..1772
FT /note="32"
FT REPEAT 1773..1779
FT /note="33"
FT REPEAT 1780..1786
FT /note="34"
FT REPEAT 1794..1799
FT /note="35; approximate"
FT REPEAT 1800..1806
FT /note="36"
FT REPEAT 1807..1813
FT /note="37"
FT DNA_BIND 326..397
FT /evidence="ECO:0000250"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..795
FT /note="Alpha-amanitin binding"
FT REGION 829..841
FT /note="Bridging helix"
FT REGION 1538..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1813
FT /note="C-terminal domain (CTD); 37 X 7 AA tandem
FT approximate repeats of Y-[GNS]-P-[QST]-[LNS]-[APT]-
FT [AGKNRSTY]"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT CONFLICT 117..122
FT /note="EEHKFK -> VCRSLFR (in Ref. 1; CAA37130)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..196
FT /note="IQRKK -> NSKEE (in Ref. 2; CAA36735)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> R (in Ref. 2; CAA36735)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="E -> R (in Ref. 2; CAA36735)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..416
FT /note="KELVDYGPHPPPGKTGA -> VRLVFISFSET (in Ref. 1;
FT CAA37130)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="L -> S (in Ref. 1; CAA37130)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="N -> D (in Ref. 1; CAA37130)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="A -> R (in Ref. 1; CAA37130)"
FT /evidence="ECO:0000305"
FT CONFLICT 1088
FT /note="A -> P (in Ref. 2; CAA36735)"
FT /evidence="ECO:0000305"
FT CONFLICT 1719
FT /note="Y -> YSPTSPSY (in Ref. 1; CAA37130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1839 AA; 204626 MW; 7B8488DBB5180B40 CRC64;
MDTRFPFSPA EVSKVRVVQF GILSPDEIRQ MSVIHVEHSE TTEKGKPKVG GLSDTRLGTI
DRKVKCETCM ANMAECPGHF GYLELAKPMY HVGFMKTVLS IMRCVCFNCS KILADEEEHK
FKQAMKIKNP KNRLKKILDA CKNKTKCDGG DDIDDVQSHS TDEPVKKSRG GCGAQQPKLT
IEGMKMIAEY KIQRKKNDEP DQLPEPAERK QTLGADRVLS VLKRISDADC QLLGFNPKFA
RPDWMILEVL PIPPPPVRPS VMMDATSRSE DDLTHQLAMI IRHNENLKRQ EKNGAPAHII
SEFTQLLQFH IATYFDNELP GQPRATQKSG RPIKSICSRL KAKEGRIRGN LMGKRVDFSA
RTVITPDPTI NIDELGVPWS IALNLTYPET VTPYNIERLK ELVDYGPHPP PGKTGAKYII
RDDGQRLDLR YLKKSSDQHL ELGYKVERHL QDGDFVLFNR QPSLHKMSIM GHRIRIMPYS
TFRLNLSVTS PYNADFDGDE MNMHVPQSFE TRAEVLELMM VPKCIVSPQA NRPVMGIVQD
TLLGCRKITK RDTFIEKDVF MNTLMWWEDF DGKVPAPAIL KPRPLWTGKQ VFNLIIPKQI
NLLRYSAWHA DTETGFITPG DTQVRIERGE LLAGTLCKKT LGTSNGSLVH VIWEEVGPDA
ARKFLGHTQW LVNYWLLQNG FTIGIGDTIA DSSTMEKINE TISNAKTAVK DLIRQFQGKE
LDPEPGRTMR DTFENRVNQV LNKARDDAGS SAQKSLAETN NLKAMVTAGS KGSFINISQM
TACVGQQNVE GKRIPFGFDG RTLPHFTKDD YGPESRGFVE NSYLRGLTPQ EFFFHAMGGR
EGLIDTAVKT SETGYIQRRL VKAMEDIMVK YDGTVRNSLG DVIQFLYGED GMDAVWIESQ
KLDSLKMKKS EFDRTFKYEI DDENWNPTYL SDEHLEDLKG IRELRDVFDA EYSKLETDRF
QLGTEIATNG DSTWPLPVNI KRHIWNAQKT FKIDLRKISD MHPVEIVDAV DKLQERLLVV
PGDDALSVEA QKNATLFFNI LLRSTLASKR VLEEYKLSRE AFEWVIGEIE SRFLQSLVAP
GEMIGCVAAQ SIGEPATQMT LNTFHYAGVS AKNVTLGVPR LREIINVAKR IKTPSLSVYL
TPEASKSKEG AKTVQCALEY TTLRSVTQAT EVWYDPDPMS TIIEEDFEFV RSYYEMPDED
VSPDKISPWL LRIELNREMM VDKKLSMADI AEKINLEFDD DLTCIFNDDN AQKLILRIRI
MNDEGPKGEL QDESAEDDVF LKKIESNMLT EMALRGIPDI NKVFIKQVRK SRFDEEGGFK
TSEEWMLDTE GVNLLAVMCH EDVDPKRTTS NHLIEIIEVL GIEAVRRALL DELRVVISFD
GSYVNYRHLA ILCDTMTYRG HLMAITRHGI NRNDTGPLMR CSFEETVDIL LDAAAYAETD
CLRGVTENIM LGQLAPIGTG DCELYLNDEM LKNAIELQLP SYMDGLEFGM TPARSPVSGT
PYHEGMMSPN YLLSPNMRLS PMSDAQFSPY VGGMAFSPSS SPGYSPSSPG YSPTSPGYSP
TSPGYSPTSP GYSPTSPTYS PSSPGYSPTS PAYSPTSPSY SPTSPSYSPT SPSYSPTSPS
YSPTSPSYSP TSPSYSPTSP AYSPTSPAYS PTSPAYSPTS PSYSPTSPSY SPTSPSYSPT
SPSYSPTSPS YSPTSPAYSP TSPGYSPTSP SYSPTSPSYG PTSPSYNPQS AKYSPSIAYS
PSNARLSPAS PYSPTSPNYS PTSPSYSPTS PSYSPSSPTY SPSSPYSSGA SPDYSPSAGY
SPTLPGYSPS STGQYTPHEG DKKDKTGKKD ASKDDKGNP
