UniProt: K9VEC1

Database: UniProt
Entry: K9VEC1_9CYAN

LinkDB:  K9VEC1_9CYAN 
Original site:  K9VEC1_9CYAN

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
   SMART (2)   
All databases (14)   

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ID   K9VEC1_9CYAN            Unreviewed;       803 AA.
AC   K9VEC1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=Osc7112_2031 {ECO:0000313|EMBL:AFZ06503.1};
OS   Oscillatoria nigro-viridis PCC 7112.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ06503.1, ECO:0000313|Proteomes:UP000010478};
RN   [1] {ECO:0000313|EMBL:AFZ06503.1, ECO:0000313|Proteomes:UP000010478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ06503.1,
RC   ECO:0000313|Proteomes:UP000010478};
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., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL   Submitted (MAY-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; CP003614; AFZ06503.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9VEC1; -.
DR   STRING; 179408.Osc7112_2031; -.
DR   KEGG; oni:Osc7112_2031; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025251_0_0_3; -.
DR   Proteomes; UP000010478; 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:UP000010478};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          534..796
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          150..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  89057 MW;  ED0FADE9669688EE CRC64;
     MRVIGCESAP KLITPNSQAK TQNSPPPNSI AHLQFKTPML LCPRCQFENP NPNKFCQQCG
     NSLIYKPCHE CGAQVAFSAA LCQNCGVATG QVWRAIICGR SNFPAVEPDE STLPPPEFPQ
     TPDIIPQTAS PQNSAEPITD SIKTEITTDA PAITVEPTSP QPSDGEFSSR EIEPVVAVGA
     IAPASFQTTE KSSNTALERE ITASEPNFTT APQPQQIQEA TENPDSPNIA DTSPPSPEFP
     IPNSEYLIPS QPAGAYLDTQ QRYQLLETVP PRKRSDTVAV KVLDCQPLEM SPLKAMLAAN
     SASVARRTSP YSAAISGENS TNPALAELCQ GIAEPYLALR WQFSQNLPVI HDSWSDNEQA
     VLLLEDCSQW PLLVERWSQP ETSTQQILYW LHEMTELWAA LEPWRCRQSL LELTNLRVNP
     DSSFSLASLR LQYLYPEPAG SNLQLVDLGQ LWQVIFSQSE HRTQFGALLD LLQQMYRGEI
     NTIEELRSRL ETVPLELQPP PSPSSTPTRR HYRSPDESPP DVGEVLTQPM PLQIYSLEDA
     GLTDVGRTRD HNEDFFSIWT QLNKIESSFG RIFQTKGLYI LCDGMGGHDS GEIASQLAAE
     TLREFFQTRW ENQLPPAETI REGVLLANKA IFEINQKDGR SGSARMGTTL VAVLVQDTQF
     AVAHVGDSRL YRLRKGQTLE KITSDHEVGQ REIKRGVDPE TAYARPDAYQ LTQAIGPRDS
     NFLKPDVQFL DLCEDTLLIL ASDGLTDNDL LETHWQNTLE PLFNPQADLD QGVAQLIELG
     NQRNGHDNIT AIIIRAQVGA FRF
//

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