ZAM_SYNY3
ID ZAM_SYNY3 Reviewed; 782 AA.
AC Q46363; P73254;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Acetazolamide conferring resistance protein zam;
GN Name=zam; OrderedLocusNames=sll1910;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7727754; DOI=10.1007/bf00020230;
RA Beuf L., Bedu S., Cami B., Joset F.;
RT "A protein is involved in accessibility of the inhibitor acetazolamide to
RT the carbonic anhydrase(s) in the cyanobacterium Synechocystis PCC 6803.";
RL Plant Mol. Biol. 27:779-788(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Not known; control resistance to the carbonic anhydrase
CC inhibitor acetazolamide.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; X80179; CAA56462.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17281.1; -; Genomic_DNA.
DR PIR; S75367; S75367.
DR AlphaFoldDB; Q46363; -.
DR SMR; Q46363; -.
DR STRING; 1148.1652358; -.
DR PaxDb; Q46363; -.
DR EnsemblBacteria; BAA17281; BAA17281; BAA17281.
DR KEGG; syn:sll1910; -.
DR eggNOG; COG0557; Bacteria.
DR InParanoid; Q46363; -.
DR PhylomeDB; Q46363; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 2.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..782
FT /note="Acetazolamide conferring resistance protein zam"
FT /id="PRO_0000166417"
FT DOMAIN 655..736
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 737..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 59
FT /note="N -> K (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..124
FT /note="EQ -> GA (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..250
FT /note="TWITA -> QDYR (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="G -> A (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="G -> E (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="G -> A (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="A -> T (in Ref. 2; BAA17281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 87542 MW; 5D12C0D6D50DFC78 CRC64;
MDYSIATLLS YFVDDKLVAG KFLEKKLGCE SPEAIEALQI ALDALEKMGV LVKERGKYNR
VTREDVVEAR LRCSSKGFCF AIQDDEDATD IYVREGNLSN AWNGDRVLVK VIKDGTRRKS
PEEQVHLILD RANPSLLAQV KKSEDNYRAV PLDDRLLFEL ELQDKEQNLG EAVDHLVHVS
VLRYPIAQHP PLGEVTKVLG SDAEAAADTD IVSCKHDLPL GWTPEAIEAL QSLPKVIEPG
ELKKRTWITA KLQLVTFGDG PRGETLPWQE VALSLESQAN QWQVGIHITD IAHYIAEDSL
LDQLARKRGT TVYLEEQICP LFPEGLIGRC SLIPDEDRLA LSFFLTVDDR GEVTGFEYHS
SVVKVDHQLD FSEVQTALAD IESVSGELKP YGGLLQELFF QICPLIKSQR LQRGSFNLQT
ETASPRLDEG RLGVIMTQET LPIRSLLAEL MVVLQREVAL QLQALGIPGL YCGQVAPEGE
DLTDIVKLAG NLDLGVKIDL EGDIIPQHYH HLSQGFESLP AKAVLNHLLA NTLKIEKYFS
HPAPHFALAY DSGYTHCVSP AQRYGDLVIQ RLLKLVLTEG RDRRTKQMKT GVELNAHTCR
NQISWNVLPP NLQETIEGDL HQLVLGLNDR EQTAEDAEKD LLGLKKAEKM KARAGEIFRG
LITGVQSYGF FVQIFDLLAE GLVHVSSLKD DWYEFRSRQC ALVGRKSRTS YRLGNEVDVQ
VRSVDYYRQQ IDLGAVNNAP KDSANMDFDD DDEDGDEREE QDTMDWDAME DGDDDEGGAV
IF