ID K9PRV4_9CYAN Unreviewed; 647 AA.
AC K9PRV4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=Cal7507_5356 {ECO:0000313|EMBL:AFY35691.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY35691.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY35691.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY35691.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003943; AFY35691.1; -; Genomic_DNA.
DR RefSeq; WP_015131482.1; NC_019682.1.
DR AlphaFoldDB; K9PRV4; -.
DR STRING; 99598.Cal7507_5356; -.
DR KEGG; calo:Cal7507_5356; -.
DR PATRIC; fig|99598.3.peg.5996; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_025251_0_0_3; -.
DR OrthoDB; 500607at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 374..637
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 647 AA; 72306 MW; AF1AFED0EDECA923 CRC64;
MLICPQCKFE NSNSNKFCQN CGTSLTHKVC PQCSTSVLVD AQNCHQCGAD CGTVWWAIIT
QEATREDSGD EGGISSLPLS SQLVVGSYLD QEQRYQLLES LPNQEETTAN KEIGLRVLDC
KPYQISPLGA MLVNQQKGLV TPSAGVSGIP CQAKPYIELK FQGHPGIPLI HDAWQQGNMQ
LVLIQDRLSW QHLLDLWKQD TTSSLQILHW CYQMTQLWSV LEPVNCRQSL LNLSNLRLDE
DQTLALRQLY VENNQSLSEP VDAEVQTVTD QEQPLTIKAL GRVWQQLFKQ SQRTQFGIIV
QMLGDLEQGK IETIAQLRSR LETIAAELEA PATEIYPLIK EKSTAAATTL LLDEAEDSSN
RNDDMPTVVL PMQLSSLEDA GRTDVGRQRH HNEDYFGIDT KLNKLELPRS RVLQARGLYI
LCDGMGGHAG GEIASELAVN TLRQYFQEHW TTKQLPTEDS IREAVYLANQ AIYDLNQQDA
RSGVGRMGTT LVMLLVQDTY AAVAHVGDSR LYRLTRKRGL EQITVDHEVG QREIARGVEA
TIAYARPDAY QLTQALGPRD EHSIKPDVEF FEINEDSLLI LASDGLSDND LLEIHWQNHL
LSLLSSGTNL EGGVTDLIDL ANQYNGHDNI TAILIRAKVR PNLDSQR
//
