ID D7E5D3_NOSA0 Unreviewed; 642 AA.
AC D7E5D3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN OrderedLocusNames=Aazo_4022 {ECO:0000313|EMBL:ADI65493.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI65493.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI65493.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI65493.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001482};
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DR EMBL; CP002059; ADI65493.1; -; Genomic_DNA.
DR RefSeq; WP_013192505.1; NC_014248.1.
DR AlphaFoldDB; D7E5D3; -.
DR STRING; 551115.Aazo_4022; -.
DR KEGG; naz:Aazo_4022; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_025251_0_0_3; -.
DR OrthoDB; 500607at2; -.
DR Proteomes; UP000001511; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR025874; DZR.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF12773; DZR; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADI65493.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 366..632
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 642 AA; 71916 MW; 6D133C14E32BD198 CRC64;
MLICPHCQFE NPNDNKFCQN CGTSLTHRAC YKCGYEVSVD TQNCQNCGAE CGTIWWAIIT
QETPVIVSEF GHALTQMQGN INSQPQSAVG SFLDREQRYQ LLAPLPSREV MATNTELKVR
VLDCQPYQIS PIEAMLGNQP DGLIVPSLSV IGIPNLAKAY VVLQPETPSV IPLIHDAWQQ
DNIQVILIED RSHWQLLLDA WQDQTTHPLQ ILHWCYQMIH LWGVLERVNC RQSLLELSNL
RLDEDQTLGL QRLHLEIPGS NLSEHAEQPL TIKALGRVWQ TLCKQSQRTQ IGSVVKMLED
LEIGKIENLE ELRSRLEEIA TELEPPANHD FSSTEAKYPS ASTILQDDDD GEEIDKNEDA
PTIILSMQLR SVENTGRTDV GRQRNHNEDY FGINSKQQKL ELPRSRNLQA RGLYILCDGM
GGHAAGEVAS ELAVSTLQQY FQENWVTAEL PTAESIQKAV FLANETIYNL NQQGLRSGVG
RMGTTLVMLL MHNTRAAVAH VGDSRLYRCT GQRGLEQITV DHEVGQREIA KGVESAIAYA
RPDAYQLTQA IGPRDANFVH PEVDFFEISE DTLLLLASDG LSDNDLVENN WQTHLEPLLS
SGANLESGLN NLIDLANEYN GHDNITGILI RVKVSPNQQS WH
//