POLH_DROME
ID POLH_DROME Reviewed; 885 AA.
AC Q9VNX1; Q9GNC0; T2GGD2;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA polymerase eta {ECO:0000312|FlyBase:FBgn0037141};
DE EC=2.7.7.7 {ECO:0000269|PubMed:11297519};
GN Name=PolH {ECO:0000312|FlyBase:FBgn0037141};
GN Synonyms=DNApol-eta {ECO:0000312|FlyBase:FBgn0037141},
GN DNApolH {ECO:0000305}, dPoleta {ECO:0000303|PubMed:11297519},
GN drad30A {ECO:0000303|PubMed:11297519, ECO:0000312|EMBL:AAF51794.1};
GN ORFNames=CG7143 {ECO:0000312|FlyBase:FBgn0037141};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:BAB15799.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF 125-ASP-GLU-126.
RX PubMed=11297519; DOI=10.1074/jbc.m009822200;
RA Ishikawa T., Uematsu N., Mizukoshi T., Iwai S., Iwasaki H., Masutani C.,
RA Hanaoka F., Ueda R., Ohmori H., Todo T.;
RT "Mutagenic and nonmutagenic bypass of DNA lesions by Drosophila DNA
RT polymerases dpoleta and dpoliota.";
RL J. Biol. Chem. 276:15155-15163(2001).
RN [2] {ECO:0000312|EMBL:BAB20905.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oshige M., Kimura S., Takata K., Sakaguchi K.;
RT "DNA polymerase eta from Drosophila melanogaster.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:AAL14000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL14000.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL14000.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000312|EMBL:AGW25604.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22532806; DOI=10.1371/journal.pgen.1002659;
RA Kane D.P., Shusterman M., Rong Y., McVey M.;
RT "Competition between replicative and translesion polymerases during
RT homologous recombination repair in Drosophila.";
RL PLoS Genet. 8:E1002659-E1002659(2012).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NOPO, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, UBIQUITINATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24553286; DOI=10.1242/dev.101196;
RA Wallace H.A., Merkle J.A., Yu M.C., Berg T.G., Lee E., Bosco G., Lee L.A.;
RT "TRIP/NOPO E3 ubiquitin ligase promotes ubiquitylation of DNA polymerase
RT eta.";
RL Development 141:1332-1341(2014).
CC -!- FUNCTION: DNA polymerase specifically involved in the DNA repair by
CC translesion synthesis (TLS) (PubMed:11297519). Plays an important role
CC in translesion synthesis, where the normal high-fidelity DNA
CC polymerases cannot proceed and DNA synthesis stalls (PubMed:11297519).
CC Inserts one or 2 nucleotide(s) opposite the lesion (PubMed:11297519).
CC During homologous recombination (HR) repair, has a overlapping role
CC with the error-prone translesion polymerase PolZ1/DNApol-zeta to
CC initiate repair synthesis that is completed by end joining or another
CC polymerase that can bind and reinitiate synthesis (PubMed:22532806).
CC Particularly important for the repair of UV-induced pyrimidine dimers
CC and for hydroxyurea (HU)-induced DNA damage (PubMed:22532806,
CC PubMed:24553286). Although inserts the correct base, may cause base
CC transitions and transversions depending upon the context (By
CC similarity). Forms a Schiff base with 5'-deoxyribose phosphate at
CC abasic sites, but does not have any lyase activity, preventing the
CC release of the 5'-deoxyribose phosphate (5'-dRP) residue (By
CC similarity). This covalent trapping of the enzyme by the 5'-dRP residue
CC inhibits its DNA synthetic activity during base excision repair,
CC thereby avoiding high incidence of mutagenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y253, ECO:0000269|PubMed:11297519,
CC ECO:0000269|PubMed:22532806, ECO:0000269|PubMed:24553286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:11297519};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC Note=Binds 2 Mg(2+). Prefers Mg(2+), but can also use Mn(2+). In vitro,
CC can also utilize other divalent cations such as Ca(2+).
CC {ECO:0000250|UniProtKB:Q9Y253};
CC -!- ACTIVITY REGULATION: The enzyme in complex with the DNA substrate binds
CC a third divalent metal cation. This binding is essential for catalyzing
CC the DNA synthesis. {ECO:0000250|UniProtKB:Q9Y253}.
CC -!- SUBUNIT: Interacts (via C-terminus) with nopo.
CC {ECO:0000269|PubMed:24553286}.
CC -!- INTERACTION:
CC Q9VNX1; Q9W0P2: Rev1; NbExp=2; IntAct=EBI-115702, EBI-95229;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24553286}.
CC Note=Localizes to interphase nuclei but undetectable during mitosis.
CC {ECO:0000269|PubMed:24553286}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries and testes.
CC {ECO:0000269|PubMed:24553286}.
CC -!- DEVELOPMENTAL STAGE: Expressed most highly in 0-2 hour embryos then at
CC lower levels in larvae and pupae. {ECO:0000269|PubMed:24553286}.
CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC subdomains, but the fingers and thumb subdomains are much smaller than
CC in high-fidelity polymerases; residues from five sequence motifs of the
CC Y-family cluster around an active site cleft that can accommodate DNA
CC and nucleotide substrates with relaxed geometric constraints, with
CC consequently higher rates of misincorporation and low processivity.
CC {ECO:0000250|UniProtKB:Q9Y253}.
CC -!- PTM: Ubiquitination enhanced by nopo. {ECO:0000269|PubMed:24553286}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:24553286). Results in
CC spindle defects (PubMed:24553286). Results in severe sensitivity of
CC third-instar larvae to ultraviolet radiation (UV) (PubMed:22532806,
CC PubMed:24553286). Exhibits a significant reduction in survival after
CC hydroxyurea (HU)-induced DNA damage (PubMed:24553286). Decreases
CC homologous recombination (HR) (PubMed:22532806). Simultaneous knockout
CC of PolH/DNApol-eta and PolZ1/DNApol-zeta does not show any difference
CC in the frequency of full HR repair compared to the single knockouts
CC suggesting they have overlapping roles (PubMed:22532806).
CC {ECO:0000269|PubMed:22532806, ECO:0000269|PubMed:24553286}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AGW25604.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB049433; BAB15799.1; -; mRNA.
DR EMBL; AB036766; BAB20905.1; -; mRNA.
DR EMBL; AE014296; AAF51794.1; -; Genomic_DNA.
DR EMBL; AY058771; AAL14000.1; -; mRNA.
DR EMBL; BT150322; AGW25604.1; ALT_INIT; mRNA.
DR RefSeq; NP_649371.2; NM_141114.3.
DR AlphaFoldDB; Q9VNX1; -.
DR SMR; Q9VNX1; -.
DR IntAct; Q9VNX1; 6.
DR STRING; 7227.FBpp0078142; -.
DR PaxDb; Q9VNX1; -.
DR EnsemblMetazoa; FBtr0078489; FBpp0078142; FBgn0037141.
DR GeneID; 40438; -.
DR KEGG; dme:Dmel_CG7143; -.
DR UCSC; CG7143-RA; d. melanogaster.
DR CTD; 40438; -.
DR FlyBase; FBgn0037141; PolH.
DR VEuPathDB; VectorBase:FBgn0037141; -.
DR eggNOG; KOG2095; Eukaryota.
DR GeneTree; ENSGT00940000157048; -.
DR HOGENOM; CLU_012348_7_2_1; -.
DR InParanoid; Q9VNX1; -.
DR OMA; MQNKYDR; -.
DR OrthoDB; 1593931at2759; -.
DR PhylomeDB; Q9VNX1; -.
DR Reactome; R-DME-110320; Translesion Synthesis by POLH.
DR BioGRID-ORCS; 40438; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40438; -.
DR PRO; PR:Q9VNX1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0037141; Expressed in adult abdomen and 19 other tissues.
DR Genevisible; Q9VNX1; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR GO; GO:0009314; P:response to radiation; IMP:FlyBase.
DR GO; GO:0019985; P:translesion synthesis; IDA:FlyBase.
DR GO; GO:0009650; P:UV protection; IMP:FlyBase.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR041298; UBZ3.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF18439; zf_UBZ; 2.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51907; ZF_UBZ3; 2.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Magnesium; Manganese; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..885
FT /note="DNA polymerase eta"
FT /id="PRO_0000448686"
FT DOMAIN 18..274
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT ZN_FING 701..737
FT /note="UBZ3-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT ZN_FING 798..832
FT /note="UBZ3-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT REGION 599..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 22
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 22
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 23
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 70
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 711
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 820
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT BINDING 824
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT MUTAGEN 125..126
FT /note="DE->AA: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:11297519"
FT CONFLICT 827
FT /note="R -> K (in Ref. 5; AAL14000, 1; BAB15799 and 2;
FT BAB20905)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="I -> T (in Ref. 5; AAL14000, 1; BAB15799 and 2;
FT BAB20905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 885 AA; 99026 MW; 79AD667CA651AC68 CRC64;
MSSARSHVSM QNKYDRVVLL VDMDCFFCQV EEKQHPEYRN RPLAVVQYNP WRGGGIIAVN
YAARAKGVTR HMRGDEAKDL CPEIVLCQVP NIREKADTSK YRDAGKEVAN VLQRFTQLLE
RASVDEAYLD ITETVNHRMQ QMQSGAFALQ PQELVNTFAV GYPSIGDYVN KITNRFANPY
MDDERYQMSY DQNDLPAVRQ SDIRLLIGAS VAGEVRAAVK KETGYECSAG IAHNKILAKL
AAGMNKPNKQ TILPLTETAS LFDSLPVGKI KGLGGKFGEV VCETLGIKFM GQVVKFSEVD
LQRKFDEKNG TWLFNISRGI DLEAVTPRFY SKSIGCCKKF PGRNNITGLK TLQHWLGELS
SEINDRLEKD FIENNRRAKH MVVQYVQDID GEEVASSRST ALRDYDQESI VRLSLDLIKA
NTKTFLRPGS ESALNNAIKF LGISVGKFET VSSGQNKLQE MFANQAAKKR RVSGDEPGQL
PKVEMEKKQK QTDEFKMKSF FANYLQGAKK EDAKADGISA NPLAAAAGAP NKNFVEEYKH
KLHAAVRTEG TVLTSTPAEF KESFFSQYLK QQKKTGQQGS VTSREDSLDV QELAEELDAI
EADNSKDFEE DTEEETELTS DTHMSKPEGQ SSDAGQEQDP NTLNDSTGND LYVETGIVPP
TLTEDELKPS TSKRKFDEIE SSVSNYKECY VEFAVPNLRT DILPTIKCDQ CGANIPDEVK
SLQTHRDHHF AQELSRTLRS TEREERTQSR QKISLKPTPP KKSKKTAGSG SSSYSTAPPS
NSITKFFRAK PTQEQAPSDP QMNQCPECKA FIKCVDMPEH LDYHVARNLQ RELNQQDLRT
RTAALNKEKI SPVQPKKQSQ KKLNSTISAS SSGTKTIAQF FSQSN
